Bifunctional protein glmU - Acinetobacter sp. (strain ADP1)

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Reviewed, UniProtKB/Swiss-Prot Q6F6U9 (GLMU_ACIAD)

Last modified February 9, 2010. Version 44. 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:	ACIAD3575

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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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_0000233720

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 – 454

207

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

Q6F6U9-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: DCC32FBE888E1DA9
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FASTA

454

49,023

        10         20         30         40         50         60 
MTTTVIILAA GKGTRMRSHL PKVLQPLAGR PLLGHVIQTA KQLNANNIIT IFGHGGAQVQ 

        70         80         90        100        110        120 
QQFQQENIQW VEQTEQLGTG HAVQMTLPVL PHDGLSLILY GDVPLVRQQT LEKLLAVSST 

       130        140        150        160        170        180 
TGIGMITLRV EDPTGYGRII RESDKIQAIV EHKDASEQQR QIQEINTGIY CVSNQKLHEW 

       190        200        210        220        230        240 
LPKLSNNNAQ GEYYLTDIVA MAVADGLEIA SIQPDLAFEV EGVNDRLQLA ALEREFQLQQ 

       250        260        270        280        290        300 
AKSLMQQGVT LTDPSRFDLR GTLKIGQDVR IDINVIIEGN CELGDFVEIG AGCVLKNTKI 

       310        320        330        340        350        360 
AAGTKVQPYS IFEDAVVGEN TQIGPFARLR PGAHLAAEVH IGNFVEVKNT SIGVGSKANH 

       370        380        390        400        410        420 
FTYLGDAEVG AGSNIGAGTI TCNYDGANKH KTVIGDAVFI GSNSSLVAPV SIGDGATVGA 

       430        440        450 
GSVITRNVPE NTLAFERAQQ IEKANYQRPQ KLKK

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References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG70216.1.
RefSeq	YP_048038.1.
3D structure databases
SMR	Q6F6U9. Positions 4-448.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6F6U9.
Genome annotation databases
GeneID	2881139.
GenomeReviews	Gene locus ACIAD3575 in contig CR543861_GR.
KEGG	aci:ACIAD3575.
NMPDR	fig\|62977.3.peg.3231.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	GSKVNHL.
PhylomeDB	Q6F6U9.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD3575-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_ACIAD

Accession

Primary (citable) accession number: Q6F6U9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 44 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