1UAE

STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008360	biological_process	regulation of cell shape
A	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE UD1 A 420

Chain	Residue
A	ASN23
A	LYS160
A	SER162
A	VAL163
A	GLY164
A	THR304
A	ASP305
A	VAL327
A	PHE328
A	ARG331
A	FFQ421
A	ARG91
A	HOH441
A	HOH541
A	HOH542
A	HOH543
A	HOH545
A	HOH557
A	HOH586
A	HOH587
A	HOH594
A	HOH608
A	TRP95
A	HOH679
A	HOH757
A	HOH802
A	ARG120
A	PRO121
A	VAL122
A	ASP123
A	LEU124
A	HIS125

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FFQ A 421

Chain	Residue
A	LYS22
A	ARG91
A	GLY114
A	CYS115
A	ARG120
A	ARG397
A	UD1420
A	HOH535
A	HOH613

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:8994972, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:1UAE, ECO:0007744|PDB:3KR6

Chain	Residue	Details
A	CYS115

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:20392080, ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3KR6, ECO:0007744|PDB:3SWD

Chain	Residue	Details
A	LYS22

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0007744|PDB:3KR6

Chain	Residue	Details
A	ARG91
A	VAL327

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6

Chain	Residue	Details
A	ARG120
A	LYS160
A	ASP305

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000305|PubMed:22378791

Chain	Residue	Details
A	CYS115

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 11027147, 11327813, 8805592, 9485407, 9890910

Chain	Residue	Details
A	ASP305
A	ARG397
A	CYS115
A	ASN23

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