CSDB glycosyltransferase search

4 glycosyltransferase activities have been found.
Please note that CSDB GT database covers only a few species: Arabidopsis thaliana, Escherichia coli, Saccharomyces cerevisiae, Acinetobacter baumannii.

Enzyme / Gene	Activity	Object	References
Enzyme name: alg13p UniProt ID: P53178* CAZy family: GT1 Gene name: ALG13 Gene GenBank ID: 852835*	Synthesized dimer: bDGlcpN(1-4)bDGlcpN Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU Acceptor (ID 34846): Ac(1-2)bDGlcpN(1-P-P-1)Subst // Subst = dolichol Status: direct evidence in vivo Confirmation methods: mutation; overexpression; in vitro (membrane preparation); in vitro (inhibition); in vitro (purified protein) ID: 247 Notes: Alg13 and Alg14 are required for the second step of lipid-linked oligosaccharide biosynthesis in Saccharomyces cerevisiae. Alg14p functions as a membrane anchor that recruits Alg13p to the cytosolic face of the ER, where catalysis of GlcNAc2-PP-dol occurs. Alg14 is a membrane protein that recruits the soluble Alg13 catalytic subunit from the cytosol to the face of the endoplasmic reticulum. Alg13p associates with Alg14p to form an active transferase catalyzing the biosynthesis of GlcNAc(2)-PP-Dol.	Organism (ID 16681,16727,16890,16891,16892,16893,16894,16895,16896,16897,16898,16899,16900,16901,16902,16903,16904,16905,16906,16907,16908,16909,16910,16911,16912,16913,16914,16915,16916,16917,16918,16919,16920,16921,16922): Saccharomyces cerevisiae SS330, W303-1A, R1158, W303a, XGY31, XGY151, XGY154, XGY155, SKY202, SKY203, XGY156, XGY158, XGY166, XGY167A, XGY168, W303-1B, MHY1409, XGY160, NAY13, WCG4a, WCG4-11/22a, NAY19, NAY20, NAY26, NAY105-1, NAY110-10.1b, NAY110-10.5d, NAY110-12.5b, NAY111-11.9a, NAY111-11.9d, NAY111-13.7c, SKY20, XGY11, ALG13-tetOp, ALG14-tetOp Full structure (ID 34847): Molecule role (precursor of): N-glycan	O’Reilly et al. 2006 DOI: 10.1021/bi060878o Chantret et al. 2005 DOI: 10.1074/jbc.M413941200 Gao et al. 2005 DOI: 10.1074/jbc.M507569200 Averbeck et al. 2008 DOI: 10.1091/mbc.E07–10–1077 Averbeck et al. 2007 DOI: 10.1074/jbc.M704410200 Lu et al. 2012 DOI: 10.1093/glycob/cwr162 Bickel et al. 2005 DOI: 10.1074/jbc.M506358200
Enzyme name: chs1p UniProt ID: P08004* CAZy family: GT2 Gene name: CHS1 Gene GenBank ID: 855529*	Synthesized dimer: bDGlcpN(1-4)bDGlcpN Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1- Status: direct evidence in vivo Confirmation methods: mutation; in vitro (crude extract); in vitro (membrane preparation); in vitro (inhibition) ID: 291 Notes: Chs1 has a secondary role as a repair enzyme, while Chs2 is mainly responsible for septum formation. Both Chs1 and Chs2 collaborate in the repair synthesis of chitin, whereas Chs1 cannot substitute for Chs2 in septum formation. The new UDP-GlcNAc competitor was found to competitively inhibit chitin synthetase from Saccharomyces cerevisiae with respect to UDP-GlcNAc, but displayed minimal antifungal activity	Organism (ID 10060,17092,17093,17094,17095): Saccharomyces cerevisiae D3C, ATCC 26109, D3A, D3B, D3D Full structure (ID 10047): CSDB ID(s): 4580, 10560, 40517, 40868, 40899, 40906, 41036, 41481, 41640, 41831, 42301, 42308, 42317, 42328, 42348, 42350, 42363, 42364, 42367, 42376, 42398, 42477, 42638, 43385, 44408, 44855, 44889, 44899, 44913, 44915, 44916, 44917, 44923, 44925, 44940, 44941, 46290, 46291, 46292, 46304, 46311, 46323, 46396, 46404, 46570, 46683, 48634, 48636, 48650, 48651, 48652, 48689, 48691, 48694, 48715, 48752, 48757, 48764, 48769, 48774, 48785, 48794, 48795, 48801, 48804, 48828, 48853, 48859, 48872, 48900, 48901, 48902, 49019, 49036, 49047, 49066, 49075, 49083, 49132, 49133, 49501, 49502, 49523, 49524, 49544, 49564, 49568, 49862, 49870, 49873, 50015, 50301, 50302, 50303, 50304, 50305, 50306, 50307, 50308, 50309, 50310, 50311, 50312, 50313, 50314, 50316, 50317, 50318, 50320, 50845, 51623, 68682, 101632, 111874, 118702, 121703, 131817, 139821, 139869, 143656, 143703, 145244, 146940, 147175, 147987, 149428, 149871, 149874, 149876 Molecule role: cell wall	Leal-Morales et al. 1994 DOI: 10.1099/13500872-140-9-2207 Bowen et al. 1992 DOI: 10.1073/pnas.89.2.519 Cabib et al. 1989 PMID: 2523889 Behr et al. 2001 DOI: 10.1080/14756360109162360 Bulawa 1992 DOI: 10.1128/mcb.12.4.1764
Enzyme name: chs2p UniProt ID: P14180* CAZy family: GT2 Gene name: CHS2 Gene GenBank ID: 852326*	Synthesized dimer: bDGlcpN(1-4)bDGlcpN Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1- Status: direct evidence in vivo Confirmation methods: mutation; in vitro (membrane preparation); in vitro (crude extract); in vitro (purified protein); overexpression ID: 292 Notes: Both Chs1 and Chs2 collaborate in the repair synthesis of chitin, whereas Chs1 cannot substitute for Chs2 in septum formation. Chitin synthase 2 has a region whose sequence is highly conserved in all chitin synthases.Substitutions of conserved amino acids in this region with alanine identified 2 domains in which any conserved amino acid could not be replaced by alanine to retain enzyme activity. Chs2 is specific for primary septum formation, whereas Chs3 is responsible for chitin in the ring at bud emergence and in the cell wall	Organism (ID 10060,10061,17093,17094,17095,17096,17097,17098,17099,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113): Saccharomyces cerevisiae D3C, ECY36-3C, D3A, D3B, D3D, RRA400-1U, YMS123+, R27-7C-1C, RRA400, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1 Full structure (ID 10047): CSDB ID(s): 40517, 43385, 44855, 44889, 44925, 46291, 46304, 139821, 149428, 149871, 149874, 149876 Molecule role: cell wall	Leal-Morales et al. 1994 DOI: 10.1099/13500872-140-9-2207 Bowen et al. 1992 DOI: 10.1073/pnas.89.2.519 Cabib et al. 1989 PMID: 2523889 Yabe et al. 1998 DOI: 10.1046/j.1432-1327.1998.2580941.x Nagahashi et al. 1995 DOI: 10.1074/jbc.270.23.13961 Uchida et al. 1996 DOI: 10.1093/oxfordjournals.jbchem.a021293 Shaw et al. 1991 PMID: 2050738
Enzyme name: chs3p UniProt ID: P29465* CAZy family: GT2 Gene name: CHS3/CAL1/CSD2/DIT101/KTI2 Gene GenBank ID: 852311*	Synthesized dimer: bDGlcpN(1-4)bDGlcpN Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1- Status: direct evidence in vivo Confirmation methods: mutation; in vitro (membrane preparation); overexpression; complementation; in vitro (membrane preparation) ID: 293 Notes: Chs3 is involved in formation of the ring of chitin found at the base of an emerging bud and of the cell wall chitin. chitin synthase III (CSIII) is responsible for the synthesis of most of the chitin found in the cell. Mutants in CHS3 gene show a defect of spore wall chitosan and a drastically reduced amount of vegetative cell wall chitin. Transformation of the mutants with a plasmid carrying CAL1 restored chitin synthase 3 activity	Organism (ID 10061,16671,16710,16803,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113,17114,17115,17116,17117,17118,17119,17120,17121,17122,17123,17124,17125,17126,17127,17128,17129,17130,17131,17132,17133,17134,17135,17136,17137,17138,17139): Saccharomyces cerevisiae ECY36-3C, W303, YPH274, PP-1A, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1, 163, 1681, 5A, 68-11, 7456-1D, AP3, CR4-2, CR4-3, HV23-3, ECY18-4B, ECY33-2A, JS163-1B, JS163-4C, JS181, JS182, PB2-1C, SHU32, TCY1, XD 1, XD 16-3B, XD 16-3D, XD16, XD17, XD18, XM33-7B, Y1170 Full structure (ID 10047): CSDB ID(s): 40517, 43385, 44855, 44889, 44925, 46291, 46304, 139821, 149428, 149871, 149874, 149876 Molecule role: cell wall	Carotti et al. 2002 DOI: 10.1002/yea.905 Bulawa 1992 DOI: 10.1128/mcb.12.4.1764 Shaw et al. 1991 PMID: 2050738 Choi et al. 1994 PMID: 8197125 Cos et al. 1998 DOI: 10.1046/j.1432-1327.1998.2560419.x Pammer et al. 1992 DOI: 10.1002/yea.320081211 Valdivieso et al. 1991 DOI: 10.1083/jcb.114.1.101

Enzyme name: alg13p
UniProt ID: P53178*

CAZy family: GT1

Gene name: ALG13
Gene GenBank ID: 852835*

Synthesized dimer: bDGlcpN(1-4)bDGlcpN

Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU

Acceptor (ID 34846): Ac(1-2)bDGlcpN(1-P-P-1)Subst // Subst = dolichol

Status: direct evidence in vivo
Confirmation methods: mutation; overexpression; in vitro (membrane preparation); in vitro (inhibition); in vitro (purified protein)

ID: 247

Notes: Alg13 and Alg14 are required for the second step of lipid-linked oligosaccharide
biosynthesis in Saccharomyces cerevisiae. Alg14p functions as a membrane anchor
that recruits Alg13p to the cytosolic face of the ER, where catalysis of GlcNAc2-PP-dol
occurs. Alg14 is a membrane protein that recruits the soluble Alg13 catalytic
subunit from the cytosol to the face of the endoplasmic reticulum. Alg13p
associates with Alg14p to form an active transferase catalyzing the biosynthesis
of GlcNAc(2)-PP-Dol.

Organism (ID 16681,16727,16890,16891,16892,16893,16894,16895,16896,16897,16898,16899,16900,16901,16902,16903,16904,16905,16906,16907,16908,16909,16910,16911,16912,16913,16914,16915,16916,16917,16918,16919,16920,16921,16922): Saccharomyces cerevisiae SS330, W303-1A, R1158, W303a, XGY31, XGY151, XGY154, XGY155, SKY202, SKY203, XGY156, XGY158, XGY166, XGY167A, XGY168, W303-1B, MHY1409, XGY160, NAY13, WCG4a, WCG4-11/22a, NAY19, NAY20, NAY26, NAY105-1, NAY110-10.1b, NAY110-10.5d, NAY110-12.5b, NAY111-11.9a, NAY111-11.9d, NAY111-13.7c, SKY20, XGY11, ALG13-tetOp, ALG14-tetOp

Full structure (ID 34847):

Molecule role (precursor of): N-glycan

O’Reilly et al. 2006
DOI: 10.1021/bi060878o

Chantret et al. 2005
DOI: 10.1074/jbc.M413941200

Gao et al. 2005
DOI: 10.1074/jbc.M507569200

Averbeck et al. 2008
DOI: 10.1091/mbc.E07–10–1077

Averbeck et al. 2007
DOI: 10.1074/jbc.M704410200

Lu et al. 2012
DOI: 10.1093/glycob/cwr162

Bickel et al. 2005
DOI: 10.1074/jbc.M506358200

Enzyme name: chs1p
UniProt ID: P08004*

CAZy family: GT2

Gene name: CHS1
Gene GenBank ID: 855529*

Synthesized dimer: bDGlcpN(1-4)bDGlcpN

Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU

Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1-

Status: direct evidence in vivo
Confirmation methods: mutation; in vitro (crude extract); in vitro (membrane preparation); in vitro (inhibition)

ID: 291

Notes: Chs1 has a secondary role as a repair enzyme, while Chs2 is mainly responsible for
septum formation. Both Chs1 and Chs2 collaborate in the repair synthesis of chitin,
whereas Chs1 cannot substitute for Chs2 in septum formation. The new UDP-GlcNAc
competitor was found to competitively inhibit chitin synthetase from Saccharomyces
cerevisiae with respect to UDP-GlcNAc, but displayed minimal antifungal
activity

Organism (ID 10060,17092,17093,17094,17095): Saccharomyces cerevisiae D3C, ATCC 26109, D3A, D3B, D3D

Full structure (ID 10047):

CSDB ID(s): 4580, 10560, 40517, 40868, 40899, 40906, 41036, 41481, 41640, 41831, 42301, 42308, 42317, 42328, 42348, 42350, 42363, 42364, 42367, 42376, 42398, 42477, 42638, 43385, 44408, 44855, 44889, 44899, 44913, 44915, 44916, 44917, 44923, 44925, 44940, 44941, 46290, 46291, 46292, 46304, 46311, 46323, 46396, 46404, 46570, 46683, 48634, 48636, 48650, 48651, 48652, 48689, 48691, 48694, 48715, 48752, 48757, 48764, 48769, 48774, 48785, 48794, 48795, 48801, 48804, 48828, 48853, 48859, 48872, 48900, 48901, 48902, 49019, 49036, 49047, 49066, 49075, 49083, 49132, 49133, 49501, 49502, 49523, 49524, 49544, 49564, 49568, 49862, 49870, 49873, 50015, 50301, 50302, 50303, 50304, 50305, 50306, 50307, 50308, 50309, 50310, 50311, 50312, 50313, 50314, 50316, 50317, 50318, 50320, 50845, 51623, 68682, 101632, 111874, 118702, 121703, 131817, 139821, 139869, 143656, 143703, 145244, 146940, 147175, 147987, 149428, 149871, 149874, 149876

Molecule role: cell wall

Leal-Morales et al. 1994
DOI: 10.1099/13500872-140-9-2207

Bowen et al. 1992
DOI: 10.1073/pnas.89.2.519

Cabib et al. 1989
PMID: 2523889

Behr et al. 2001
DOI: 10.1080/14756360109162360

Bulawa 1992
DOI: 10.1128/mcb.12.4.1764

Enzyme name: chs2p
UniProt ID: P14180*

CAZy family: GT2

Gene name: CHS2
Gene GenBank ID: 852326*

Synthesized dimer: bDGlcpN(1-4)bDGlcpN

Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU

Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1-

Status: direct evidence in vivo
Confirmation methods: mutation; in vitro (membrane preparation); in vitro (crude extract); in vitro (purified protein); overexpression

ID: 292

Notes: Both Chs1 and Chs2 collaborate in the repair synthesis of chitin, whereas Chs1 cannot
substitute for Chs2 in septum formation. Chitin synthase 2 has a region whose
sequence is highly conserved in all chitin synthases.Substitutions of conserved
amino acids in this region with alanine identified 2 domains in which any conserved
amino acid could not be replaced by alanine to retain enzyme activity. Chs2
is specific for primary septum formation, whereas Chs3 is responsible for chitin
in the ring at bud emergence and in the cell wall

Organism (ID 10060,10061,17093,17094,17095,17096,17097,17098,17099,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113): Saccharomyces cerevisiae D3C, ECY36-3C, D3A, D3B, D3D, RRA400-1U, YMS123+, R27-7C-1C, RRA400, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1

Full structure (ID 10047):

CSDB ID(s): 40517, 43385, 44855, 44889, 44925, 46291, 46304, 139821, 149428, 149871, 149874, 149876

Molecule role: cell wall

Leal-Morales et al. 1994
DOI: 10.1099/13500872-140-9-2207

Bowen et al. 1992
DOI: 10.1073/pnas.89.2.519

Cabib et al. 1989
PMID: 2523889

Yabe et al. 1998
DOI: 10.1046/j.1432-1327.1998.2580941.x

Nagahashi et al. 1995
DOI: 10.1074/jbc.270.23.13961

Uchida et al. 1996
DOI: 10.1093/oxfordjournals.jbchem.a021293

Shaw et al. 1991
PMID: 2050738

Enzyme name: chs3p
UniProt ID: P29465*

CAZy family: GT2

Gene name: CHS3/CAL1/CSD2/DIT101/KTI2
Gene GenBank ID: 852311*

Synthesized dimer: bDGlcpN(1-4)bDGlcpN

Donor (ID 33944): Ac(1-2)?DGlcpN(1-P-P-5)xXnucU

Acceptor (ID 34894): -4)[Ac(1-2)]bDGlcpN(1-

Status: direct evidence in vivo
Confirmation methods: mutation; in vitro (membrane preparation); overexpression; complementation; in vitro (membrane preparation)

ID: 293

Notes: Chs3 is involved in formation of the ring of chitin found at the base of an emerging
bud and of the cell wall chitin. chitin synthase III (CSIII) is responsible
for the synthesis of most of the chitin found in the cell. Mutants in CHS3 gene
show a defect of spore wall chitosan and a drastically reduced amount of vegetative
cell wall chitin. Transformation of the mutants with a plasmid carrying CAL1
restored chitin synthase 3 activity

Organism (ID 10061,16671,16710,16803,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113,17114,17115,17116,17117,17118,17119,17120,17121,17122,17123,17124,17125,17126,17127,17128,17129,17130,17131,17132,17133,17134,17135,17136,17137,17138,17139): Saccharomyces cerevisiae ECY36-3C, W303, YPH274, PP-1A, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1, 163, 1681, 5A, 68-11, 7456-1D, AP3, CR4-2, CR4-3, HV23-3, ECY18-4B, ECY33-2A, JS163-1B, JS163-4C, JS181, JS182, PB2-1C, SHU32, TCY1, XD 1, XD 16-3B, XD 16-3D, XD16, XD17, XD18, XM33-7B, Y1170

Full structure (ID 10047):

CSDB ID(s): 40517, 43385, 44855, 44889, 44925, 46291, 46304, 139821, 149428, 149871, 149874, 149876

Molecule role: cell wall

Carotti et al. 2002
DOI: 10.1002/yea.905

Bulawa 1992
DOI: 10.1128/mcb.12.4.1764

Shaw et al. 1991
PMID: 2050738

Choi et al. 1994
PMID: 8197125

Cos et al. 1998
DOI: 10.1046/j.1432-1327.1998.2560419.x

Pammer et al. 1992
DOI: 10.1002/yea.320081211

Valdivieso et al. 1991
DOI: 10.1083/jcb.114.1.101

#GTR ID	Enzyme name	Enzyme group	Enzyme Genbank ID	Derived ID mark	Enzyme Uniprot ID	Derived ID mark	CAZY family	Gene name	Gene Genbank ID	Derived ID mark	Gene cluster	Full structure CSDB structure ID	Side product CSDB structure ID	Full structure	Full structure is fragment (0|1)	Synthesized bond	Synthesized bond location (from root ~ subst position)	Donor structure ID	Substrate structure	Confirmation status	Methods used	Notes	Molecule role	Molecule is a model of role (0|1)	Molecule is a precursor of role (0|1)	Main CSDB record ID	Additional CSDB record IDs	CSDB organism IDs	Organism names	Organs and tissues	References (;-separated)
247	alg13p				P53178	*	GT1	ALG13	852835	*		34847		Ac(1-2)bDGlcpN(1-4)[Ac(1-2)]bDGlcpN(1-P-P-1)Subst // Subst = dolichol	0	bDGlcpN(1-4)bDGlcpN	4~4	Ac(1-2)?DGlcpN(1-P-P-5)xXnucU	Ac(1-2)bDGlcpN(1-P-P-1)Subst // Subst = dolichol	in vivo	mutation; overexpression; in vitro (membrane preparation); in vitro (inhibition); in vitro (purified protein)	Alg13 and Alg14 are required for the second step of lipid-linked oligosaccharide biosynthesis in Saccharomyces cerevisiae. Alg14p functions as a membrane anchor that recruits Alg13p to the cytosolic face of the ER, where catalysis of GlcNAc2-PP-dol occurs. Alg14 is a membrane protein that recruits the soluble Alg13 catalytic subunit from the cytosol to the face of the endoplasmic reticulum. Alg13p associates with Alg14p to form an active transferase catalyzing the biosynthesis of GlcNAc(2)-PP-Dol.	N-glycan	0	1			16681,16727,16890,16891,16892,16893,16894,16895,16896,16897,16898,16899,16900,16901,16902,16903,16904,16905,16906,16907,16908,16909,16910,16911,16912,16913,16914,16915,16916,16917,16918,16919,16920,16921,16922	Saccharomyces cerevisiae SS330, W303-1A, R1158, W303a, XGY31, XGY151, XGY154, XGY155, SKY202, SKY203, XGY156, XGY158, XGY166, XGY167A, XGY168, W303-1B, MHY1409, XGY160, NAY13, WCG4a, WCG4-11/22a, NAY19, NAY20, NAY26, NAY105-1, NAY110-10.1b, NAY110-10.5d, NAY110-12.5b, NAY111-11.9a, NAY111-11.9d, NAY111-13.7c, SKY20, XGY11, ALG13-tetOp, ALG14-tetOp		O’Reilly et al. 2006 (doi: 10.1021/bi060878o); Chantret et al. 2005 (doi: 10.1074/jbc.M413941200); Gao et al. 2005 (doi: 10.1074/jbc.M507569200); Averbeck et al. 2008 (doi: 10.1091/mbc.E07–10–1077); Averbeck et al. 2007 (doi: 10.1074/jbc.M704410200); Lu et al. 2012 (doi: 10.1093/glycob/cwr162); Bickel et al. 2005 (doi: 10.1074/jbc.M506358200)	
291	chs1p				P08004	*	GT2	CHS1	855529	*		10047		-4)[Ac(1-2)]bDGlcpN(1-	0	bDGlcpN(1-4)bDGlcpN	1~4	Ac(1-2)?DGlcpN(1-P-P-5)xXnucU	-4)[Ac(1-2)]bDGlcpN(1-	in vivo	mutation; in vitro (crude extract); in vitro (membrane preparation); in vitro (inhibition)	Chs1 has a secondary role as a repair enzyme, while Chs2 is mainly responsible for septum formation. Both Chs1 and Chs2 collaborate in the repair synthesis of chitin, whereas Chs1 cannot substitute for Chs2 in septum formation. The new UDP-GlcNAc competitor was found to competitively inhibit chitin synthetase from Saccharomyces cerevisiae with respect to UDP-GlcNAc, but displayed minimal antifungal activity	cell wall	0	0		4580,10560,40517,40868,40899,40906,41036,41481,41640,41831,42301,42308,42317,42328,42348,42350,42363,42364,42367,42376,42398,42477,42638,43385,44408,44855,44889,44899,44913,44915,44916,44917,44923,44925,44940,44941,46290,46291,46292,46304,46311,46323,46396,46404,46570,46683,48634,48636,48650,48651,48652,48689,48691,48694,48715,48752,48757,48764,48769,48774,48785,48794,48795,48801,48804,48828,48853,48859,48872,48900,48901,48902,49019,49036,49047,49066,49075,49083,49132,49133,49501,49502,49523,49524,49544,49564,49568,49862,49870,49873,50015,50301,50302,50303,50304,50305,50306,50307,50308,50309,50310,50311,50312,50313,50314,50316,50317,50318,50320,50845,51623,68682,101632,111874,118702,121703,131817,139821,139869,143656,143703,145244,146940,147175,147987,149428,149871,149874,149876	10060,17092,17093,17094,17095	Saccharomyces cerevisiae D3C, ATCC 26109, D3A, D3B, D3D		Leal-Morales et al. 1994 (doi: 10.1099/13500872-140-9-2207); Bowen et al. 1992 (doi: 10.1073/pnas.89.2.519); Cabib et al. 1989 (doi:    pmid: 2523889); Behr et al. 2001 (doi: 10.1080/14756360109162360); Bulawa 1992 (doi: 10.1128/mcb.12.4.1764)	
292	chs2p				P14180	*	GT2	CHS2	852326	*		10047		-4)[Ac(1-2)]bDGlcpN(1-	0	bDGlcpN(1-4)bDGlcpN	1~4	Ac(1-2)?DGlcpN(1-P-P-5)xXnucU	-4)[Ac(1-2)]bDGlcpN(1-	in vivo	mutation; in vitro (membrane preparation); in vitro (crude extract); in vitro (purified protein); overexpression	Both Chs1 and Chs2 collaborate in the repair synthesis of chitin, whereas Chs1 cannot substitute for Chs2 in septum formation. Chitin synthase 2 has a region whose sequence is highly conserved in all chitin synthases.Substitutions of conserved amino acids in this region with alanine identified 2 domains in which any conserved amino acid could not be replaced by alanine to retain enzyme activity. Chs2 is specific for primary septum formation, whereas Chs3 is responsible for chitin in the ring at bud emergence and in the cell wall	cell wall	0	0		40517,43385,44855,44889,44925,46291,46304,139821,149428,149871,149874,149876	10060,10061,17093,17094,17095,17096,17097,17098,17099,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113	Saccharomyces cerevisiae D3C, ECY36-3C, D3A, D3B, D3D, RRA400-1U, YMS123+, R27-7C-1C, RRA400, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1		Leal-Morales et al. 1994 (doi: 10.1099/13500872-140-9-2207); Bowen et al. 1992 (doi: 10.1073/pnas.89.2.519); Cabib et al. 1989 (doi:    pmid: 2523889); Yabe et al. 1998 (doi: 10.1046/j.1432-1327.1998.2580941.x); Nagahashi et al. 1995 (doi: 10.1074/jbc.270.23.13961); Uchida et al. 1996 (doi: 10.1093/oxfordjournals.jbchem.a021293); Shaw et al. 1991 (doi:    pmid: 2050738)	
293	chs3p				P29465	*	GT2	CHS3/CAL1/CSD2/DIT101/KTI2	852311	*		10047		-4)[Ac(1-2)]bDGlcpN(1-	0	bDGlcpN(1-4)bDGlcpN	1~4	Ac(1-2)?DGlcpN(1-P-P-5)xXnucU	-4)[Ac(1-2)]bDGlcpN(1-	in vivo	mutation; in vitro (membrane preparation); overexpression; complementation; in vitro (membrane preparation)	Chs3 is involved in formation of the ring of chitin found at the base of an emerging bud and of the cell wall chitin. chitin synthase III (CSIII) is responsible for the synthesis of most of the chitin found in the cell. Mutants in CHS3 gene show a defect of spore wall chitosan and a drastically reduced amount of vegetative cell wall chitin. Transformation of the mutants with a plasmid carrying CAL1 restored chitin synthase 3 activity	cell wall	0	0		40517,43385,44855,44889,44925,46291,46304,139821,149428,149871,149874,149876	10061,16671,16710,16803,17100,17101,17102,17103,17104,17105,17106,17107,17108,17109,17110,17111,17112,17113,17114,17115,17116,17117,17118,17119,17120,17121,17122,17123,17124,17125,17126,17127,17128,17129,17130,17131,17132,17133,17134,17135,17136,17137,17138,17139	Saccharomyces cerevisiae ECY36-3C, W303, YPH274, PP-1A, ECY33-16C, ECY33-18A, ECY19A2-5B, ECY36-3A, ECY36-3D, ASY2, ASY2-24A, ASY2-24B, ASY2-24C, ASY2-24D, EMY12-1C, EMY13-2C, H182-6-3, H102-3-1, 163, 1681, 5A, 68-11, 7456-1D, AP3, CR4-2, CR4-3, HV23-3, ECY18-4B, ECY33-2A, JS163-1B, JS163-4C, JS181, JS182, PB2-1C, SHU32, TCY1, XD 1, XD 16-3B, XD 16-3D, XD16, XD17, XD18, XM33-7B, Y1170		Carotti et al. 2002 (doi: 10.1002/yea.905); Bulawa 1992 (doi: 10.1128/mcb.12.4.1764); Shaw et al. 1991 (doi:    pmid: 2050738); Choi et al. 1994 (doi:    pmid: 8197125); Cos et al. 1998 (doi: 10.1046/j.1432-1327.1998.2560419.x); Pammer et al. 1992 (doi: 10.1002/yea.320081211); Valdivieso et al. 1991 (doi: 10.1083/jcb.114.1.101)