Bifunctional protein glmU - Azoarcus sp. (strain BH72)

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Reviewed, UniProtKB/Swiss-Prot A1KBP7 (GLMU_AZOSB)

Last modified February 9, 2010. Version 28. 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:	azo3637

Organism

Azoarcus sp. (strain BH72) [Complete proteome] [HAMAP]

Taxonomic identifier

62928 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Azoarcus

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Protein attributes

Sequence length	452 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 – 452

452

Bifunctional protein glmU HAMAP MF_01631

PRO_1000056137

Regions

Region

1 – 225

225

Pyrophosphorylase By similarity

Region

6 – 9

Substrate binding By similarity

Region

76 – 77

Substrate binding By similarity

Region

226 – 246

Linker By similarity

Region

247 – 452

206

N-acetyltransferase By similarity

Sites

Active site

359

Proton acceptor By similarity

Metal binding

100

Magnesium By similarity

Metal binding

223

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

135

Substrate; via amide nitrogen By similarity

Binding site

150

Substrate By similarity

Binding site

165

Substrate By similarity

Binding site

383

Acetyl-CoA By similarity

Binding site

401

Acetyl-CoA By similarity

Binding site

419

Acetyl-CoA; via amide nitrogen By similarity

Binding site

436

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

A1KBP7-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3F92AB324E0F9A9A
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FASTA

452

48,486

        10         20         30         40         50         60 
MEVVILAAGQ GKRMRSVLPK VLQPLAGKPM LSHVLDAART LAARRICVVY GHGGEVVRER 

        70         80         90        100        110        120 
LDAADLAWAR QEPQLGTGHA VQQALPHLTD GDLALVLYGD VPLIGVPTLQ RLAAAAGDTR 

       130        140        150        160        170        180 
LALLTVELDN PTGYGRILRD AAGRVVRIVE EKDASDAERR VREVNTGILV APVARLRAWL 

       190        200        210        220        230        240 
GSLRNDNAQG EYYLTDIIGM AVAEDIEVVT VQPDAVSETL GVNSKPQLAE LERIHQRNIA 

       250        260        270        280        290        300 
QRLMEDGVTL IDPARIDVRG ELVCGRDVEI DVNCVFEGRV ELGDGVRIGA NCVVRDARIG 

       310        320        330        340        350        360 
SGTRVAPFSH IEQTVMGPAC VIGPYARTRP GTELGEDVHL GNFVEVKNSV IAAHSKANHL 

       370        380        390        400        410        420 
AYVGDADVGQ RVNIGAGTIT CNYDGANKFR TVIEDDVFIG SDTQLVAPVR VGRGATLGAG 

       430        440        450 
TTLTKDAPPE QLTVSRAKQL SIAGWKRPVK QR

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References

[1]

"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S.

Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AM406670 Genomic DNA. Translation: CAL96253.1.
RefSeq	YP_935139.1.
3D structure databases
SMR	A1KBP7. Positions 1-447.
ModBase	Search...
Protein-protein interaction databases
STRING	A1KBP7.
Genome annotation databases
GeneID	4608892.
GenomeReviews	Gene locus azo3637 in contig AM406670_GR.
KEGG	azo:azo3637.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	A1KBP7.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. 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. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

GLMU_AZOSB

Accession

Primary (citable) accession number: A1KBP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	February 9, 2010
This is version 28 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

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents