Q9A5Z3 (GLMU_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein GlmU

Including the following 2 domains:

1. UDP-N-acetylglucosamine pyrophosphorylase
   EC=2.7.7.23
   Alternative name(s):
   N-acetylglucosamine-1-phosphate uridyltransferase
2. Glucosamine-1-phosphate N-acetyltransferase
   EC=2.3.1.157

Gene names

Name:	glmU
Ordered Locus Names:	CC_2304

Organism

Caulobacter crescentus (Caulobacter vibrioides)

Taxonomic identifier

155892 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc By similarity. HAMAP MF_01631
Catalytic activity	Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP MF_01631 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. HAMAP MF_01631
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01631
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631 Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_01631
Subcellular location	Cytoplasm By similarity HAMAP MF_01631.
Sequence similarities	In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Magnesium Metal-binding
Molecular function	Acyltransferase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	cell morphogenesis Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylglucosamine diphosphorylase activity Inferred from electronic annotation. Source: EC glucosamine-1-phosphate N-acetyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Bifunctional protein GlmU HAMAP MF_01631		PRO_0000233754
Regions
	Region	1 – 239	239	Pyrophosphorylase By similarity
	Region	17 – 20	4	Substrate binding By similarity
	Region	89 – 90	2	Substrate binding By similarity
	Region	240 – 260	21	Linker By similarity
	Region	261 – 462	202	N-acetyltransferase By similarity
Sites
	Active site	356	1	Proton acceptor By similarity
	Metal binding	114	1	Magnesium By similarity
	Metal binding	237	1	Magnesium By similarity
	Binding site	84	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	180	1	Substrate By similarity
	Binding site	380	1	Acetyl-CoA By similarity
	Binding site	398	1	Acetyl-CoA By similarity
	Binding site	433	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9A5Z3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 84FCE7C136972D3B	FASTA	462	48,191
	10 20 30 40 50 60 MTESVSKPVR PRAAVILAAG QGTRMKSPTP KVLHRLAGRT LLDHAIDAAE GLGCERIIVV 70 80 90 100 110 120 VGAHSPQVGE SARKRLGPDA TVIQDPPLGT GHAVLAAKDA LADFHGDVVV TYADCPLTTA 130 140 150 160 170 180 PVIAPLFDLI THVAHVAVLG FEAQNPTGYG RLILAPGHVL LRIVEEKEAD LATKQVKHCN 190 200 210 220 230 240 SGVLAADRAV LFDLLANVRN DNAKGEYYLT DVVGLAHERH LSTRTAFAPE ASVQGVNAQA 250 260 270 280 290 300 ELAAAEAVWQ QNRRKALMVD GVTMPAPDTV HLAWDTQIAG GAVVEQFVVF GPGVSVASGA 310 320 330 340 350 360 VIKAFSHLEG AVVGEGALIG PYARLRPGAE IGPDAHIGNF VEVKKVKVGA GAKANHLSYL 370 380 390 400 410 420 GDGSVGEKAN IGAGTIFCNY DGFEKFETHV GKGAFIGSNS ALVAPVRVGD GAMTGSGSVI 430 440 450 460 TKDVEDGALA LSRADQTSKA GWATKFRAIK QAQKDKKKDK KA

References

[1]

"Complete genome sequence of Caulobacter crescentus." Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J. , Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001) [PubMed: 11259647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19089 / CB15.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005673 Genomic DNA. Translation: AAK24275.1.
PIR	G87534.
RefSeq	NP_421107.1. NC_002696.2.
3D structure databases
ProteinModelPortal	Q9A5Z3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	941054.
GenomeReviews	Gene locus CC_2304 in contig AE005673_GR.
KEGG	ccr:CC_2304.
NMPDR	fig|190650.1.peg.2287.
PATRIC	21301632. VBICauCre124313_2323.
TIGR	CC_2304.
Phylogenomic databases
HOGENOM	HBG688195.
OMA	GSKVNHL.
ProtClustDB	PRK14353.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. IPR001451. Hexapep_transf. IPR011004. Trimer_LpxA-like. [Graphical view]
KO	K04042.
PANTHER	PTHR22572:SF17. PTHR22572:SF17. 1 hit.
Pfam	PF00132. Hexapep. 2 hits. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR01173. GlmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_CAUCR

Accession

Primary (citable) accession number: Q9A5Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program