Bifunctional protein glmU - Bartonella tribocorum (strain CIP 105476 / IBS 506)

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Reviewed, UniProtKB/Swiss-Prot A9IVJ6 (GLMU_BART1)

Last modified February 9, 2010. Version 21. 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:	BT_1367

Organism

Bartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]

Taxonomic identifier

382640 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

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Protein attributes

Sequence length	454 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 – 454

454

Bifunctional protein glmU HAMAP MF_01631

PRO_0000337710

Regions

Region

1 – 231

231

Pyrophosphorylase By similarity

Region

82 – 83

Substrate binding By similarity

Region

232 – 252

Linker By similarity

Region

253 – 454

202

N-acetyltransferase By similarity

Sites

Active site

348

Proton acceptor By similarity

Metal binding

107

Magnesium By similarity

Metal binding

229

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

143

Substrate; via amide nitrogen By similarity

Binding site

157

Substrate By similarity

Binding site

172

Substrate By similarity

Binding site

372

Acetyl-CoA By similarity

Binding site

390

Acetyl-CoA By similarity

Binding site

408

Acetyl-CoA; via amide nitrogen By similarity

Binding site

425

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

A9IVJ6-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 6159609382103339
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FASTA

454

49,347

        10         20         30         40         50         60 
MVRSCLSIVL SAGEGTRMKS PLPKVLHKIA GLPLICHVLK QIELAESSQV AVVVGCGGQE 

        70         80         90        100        110        120 
VTHVVQSFVK DVMIFEQKER LGTAHAVLSA RFALQKGVDD ILIVFGDTPL IQQESLHQMR 

       130        140        150        160        170        180 
AQLADGADVV FAGFHTQDPT GYGRLLEKNG QLIAIVEEKD ASEEEKKISF CNGGILAMRG 

       190        200        210        220        230        240 
KHALSLLEKV DNNNMKKEYY LTDIASLASR EGLDVRVVEV PFENIVGINN CLELSRADSL 

       250        260        270        280        290        300 
WQKRKARDLM LSGVTLLKPE TVYFSYDTEI EPGVVIEPNV YFGLGVKVQS GAVIRAFSYL 

       310        320        330        340        350        360 
EGAVVGQDAQ IGPYARLRPG TELAKSVKVG NFCEVKQAKV GESSKINHLS YIGDAEIGAH 

       370        380        390        400        410        420 
TNIGAGTITC NYDGFNKYKT VIGDHAFVGS NTALVSPLVI GDGSYVASGS VITENIPMNS 

       430        440        450 
MAFGRARQVI KEGYATKFRA RLLEKNLSEN KQKK

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References

[1]

"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AM260525 Genomic DNA. Translation: CAK01729.1.
RefSeq	YP_001609724.1.
3D structure databases
SMR	A9IVJ6. Positions 4-435.
ModBase	Search...
Genome annotation databases
GeneID	5829022.
GenomeReviews	Gene locus BT_1367 in contig AM260525_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG688195.
OMA	GSKVNHL.
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. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

GLMU_BART1

Accession

Primary (citable) accession number: A9IVJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	February 9, 2010
This is version 21 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents