Bifunctional protein glmU - Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240)

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Reviewed, UniProtKB/Swiss-Prot A0KQX6 (GLMU_AERHH)

Last modified February 9, 2010. Version 29. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Bifunctional protein glmU
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            N-acetylglucosamine-1-phosphate uridyltransferase
    2- Recommended name:
            Glucosamine-1-phosphate N-acetyltransferase
              EC=2.3.1.157

Gene names

Name:	glmU
Ordered Locus Names:	AHA_4260

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

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Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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.

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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
Gene Ontology (GO)
Biological process	cell morphogenesis Inferred from electronic annotation. Source: HAMAP 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: HAMAP 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: HAMAP glucosamine-1-phosphate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Bifunctional protein glmU HAMAP MF_01631

PRO_1000056135

Regions

Region

1 – 226

226

Pyrophosphorylase By similarity

Region

8 – 11

Substrate binding By similarity

Region

78 – 79

Substrate binding By similarity

Region

227 – 247

Linker By similarity

Region

248 – 453

206

N-acetyltransferase By similarity

Sites

Active site

360

Proton acceptor By similarity

Metal binding

102

Magnesium By similarity

Metal binding

224

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

137

Substrate; via amide nitrogen By similarity

Binding site

151

Substrate By similarity

Binding site

166

Substrate By similarity

Binding site

384

Acetyl-CoA By similarity

Binding site

402

Acetyl-CoA By similarity

Binding site

420

Acetyl-CoA; via amide nitrogen By similarity

Binding site

437

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

A0KQX6-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 135D868733BD5685
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FASTA

453

48,788

        10         20         30         40         50         60 
MSLNVVILAA GKGTRMRSSL PKVLHPVANK PMVSHVIETA RKVGAEQLHL VYGHGAELLK 

        70         80         90        100        110        120 
ERIQASDLNW VLQAQQLGTG HAVAQAIPFW QDEDDVLVLY GDTPLIQPET LQRLLAAKAS 

       130        140        150        160        170        180 
DGMALLTVVL DNPTGYGRIV RSNGQVVGIV EQKDANAEQL AIREVNTGVL VANGGQLRSW 

       190        200        210        220        230        240 
LSRLDNKNAQ GEFYLTDVIA MAHADNCPIA AVHPDDAMEV EGANNRVQLA QLERSYQKMQ 

       250        260        270        280        290        300 
AERLMIAGAT LIDPARFDLR GTLEIGEEVV IDVNVIIEGK VVLGNHVRIG AGSVLKDCVI 

       310        320        330        340        350        360 
GDHSEVKPYS VIEGAQIADQ CSVGPFTRLR PGTVLEQDAH VGNFVEMKKA RLGVGSKCGH 

       370        380        390        400        410        420 
LTYLGDAEVG AKVNIGAGTI TCNYDGVNKF QTIIEDDVFV GSDTQLVAPV RIGKGATLGA 

       430        440        450 
GSTITKDVAE NELVITRVPQ RHIQNWARPV KKK

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References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000462 Genomic DNA. Translation: ABK38010.1.
RefSeq	YP_858677.1.
3D structure databases
SMR	A0KQX6. Positions 2-450.
ModBase	Search...
Protein-protein interaction databases
STRING	A0KQX6.
Genome annotation databases
GeneID	4487364.
GenomeReviews	Gene locus AHA_4260 in contig CP000462_GR.
KEGG	aha:AHA_4260.
TIGR	AHA_4260.
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	A0KQX6.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. IPR018357. Hexapep_transf_CS. IPR005835. NTP_transferase. IPR011004. Trimer_LpxA-like. [Graphical view]
Pfam	PF00483. NTP_transferase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 2 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

GLMU_AERHH

Accession

Primary (citable) accession number: A0KQX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 12, 2006
Last modified:	February 9, 2010
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents