Bifunctional protein glmU - Blochmannia floridanus

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Reviewed, UniProtKB/Swiss-Prot Q7VQV4 (GLMU_BLOFL)

Last modified February 9, 2010. Version 47. 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:	Bfl010

Organism

Blochmannia floridanus [Complete proteome] [HAMAP]

Taxonomic identifier

203907 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

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Protein attributes

Sequence length	465 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 – 465

465

Bifunctional protein glmU HAMAP MF_01631

PRO_0000233738

Regions

Region

1 – 237

237

Pyrophosphorylase By similarity

Region

11 – 14

Substrate binding By similarity

Region

85 – 86

Substrate binding By similarity

Region

238 – 258

Linker By similarity

Region

259 – 465

207

N-acetyltransferase By similarity

Sites

Active site

371

Proton acceptor By similarity

Metal binding

110

Magnesium By similarity

Metal binding

235

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

145

Substrate; via amide nitrogen By similarity

Binding site

160

Substrate By similarity

Binding site

395

Acetyl-CoA By similarity

Binding site

431

Acetyl-CoA; via amide nitrogen By similarity

Binding site

448

Acetyl-CoA By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7VQV4-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F651C7E6DEF99D8D
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FASTA

465

51,831

        10         20         30         40         50         60 
MLRKKYSVII LAAGQGKRML SSIPKVMHKI AGRSMLQHLI DSVSKINIQS IYIVYNESLR 

        70         80         90        100        110        120 
EFIPTIYSNK CTISIYWVLQ ESVRGTGYAV QQVLSMIHDD NEDILILYGD VPLISDKTLN 

       130        140        150        160        170        180 
NLCLMKSKCD IGLLTAYVKN PQGYGRIIRN QYGDVVSIIE DIDIVNQNDR IIKEIHSGIF 

       190        200        210        220        230        240 
ISVSGYLKSW LNYLIENNLW CNELYLTAII DIAYKNNFVI NAIHPVDVCE VIGINNKSDL 

       250        260        270        280        290        300 
VKAERVYQIK EAQKLLELGV MISDLNRFDL RGKLVCGEDV CIDVNVIIEG CVSLGNRVKI 

       310        320        330        340        350        360 
GASCILKDVE IGDDVIIYPF SFIENSKIHC KSKIGPFARL RPGTCLQEQV HIGNFVELKN 

       370        380        390        400        410        420 
IKLGNNSKVG HLSYLGDADV GNYVNIGAGT IICNYNGKTK NYTCIEDNVF VGADSQLVAP 

       430        440        450        460 
ITIGKNAVIG AGTTVTQNVD KDDVIISRVR QFSIVNDKVD KNKKN

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References

[1]

"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248583 Genomic DNA. Translation: CAD83538.1.
RefSeq	NP_878325.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7VQV4.
Genome annotation databases
GeneID	1499210.
GenomeReviews	Gene locus Bfl010 in contig BX248583_GR.
KEGG	bfl:Bfl010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	Q7VQV4.
Enzyme and pathway databases
BioCyc	CBLO203907:BFL010-MONOMER.
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_BLOFL

Accession

Primary (citable) accession number: Q7VQV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 47 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents