3FWW

The crystal structure of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase from Yersinia pestis CO92

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000902	biological_process	cell morphogenesis
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0008360	biological_process	regulation of cell shape
A	0009245	biological_process	lipid A biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019134	molecular_function	glucosamine-1-phosphate N-acetyltransferase activity
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization

Functional Information from PROSITE/UniProt

site_id	PS00101
Number of Residues	29
Details	HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVtVAngAtIGagTtVtrdV

Chain	Residue	Details
A	VAL403-VAL431

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631

Chain	Residue	Details
A	HIS363

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site_id	SWS_FT_FI2
Number of Residues	19
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631

Chain	Residue	Details
A	GLN76
A	GLY81
A	TYR103
A	ASP105
A	GLY140
A	GLU154
A	ASN169
A	ASN227
A	ARG333
A	LYS351
A	TYR366
A	ASN377
A	ALA380
A	ASN386
A	SER405
A	ALA423
A	ARG440
A	LEU11
A	LYS25

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