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E3IID5 (E3IID5_GEOS0) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU HAMAP-Rule MF_01631
Gene names
Name:glmU HAMAP-Rule MF_01631
Ordered Locus Names:GY4MC1_0046 EMBL ADP72902.1
OrganismGeobacillus sp. (strain Y4.1MC1) [Complete proteome] [HAMAP] EMBL ADP72902.1
Taxonomic identifier581103 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity. HAMAP-Rule MF_01631 SAAS SAAS005835

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631 SAAS SAAS005835

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631 SAAS SAAS005835

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01631

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP-Rule MF_01631 SAAS SAAS005835

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-Rule MF_01631 SAAS SAAS005835

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. HAMAP-Rule MF_01631 SAAS SAAS005835

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631 SAAS SAAS005835

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01631.

Sequence similarities

In the C-terminal section; belongs to the transferase hexapeptide repeat family. HAMAP-Rule MF_01631

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. HAMAP-Rule MF_01631

Ontologies

Keywords
   Biological processCell shape
Cell wall biogenesis/degradation HAMAP-Rule MF_01631 SAAS SAAS005835
Peptidoglycan synthesis HAMAP-Rule MF_01631 SAAS SAAS005835
   Cellular componentCytoplasm HAMAP-Rule MF_01631 SAAS SAAS005835
   DomainRepeat HAMAP-Rule MF_01631 SAAS SAAS005835
   LigandMagnesium HAMAP-Rule MF_01631 SAAS SAAS005835
Metal-binding HAMAP-Rule MF_01631 SAAS SAAS005835
   Molecular functionAcyltransferase HAMAP-Rule MF_01631 SAAS SAAS005835
Nucleotidyltransferase HAMAP-Rule MF_01631 SAAS SAAS005835
Transferase
   Technical termComplete proteome
Multifunctional enzyme HAMAP-Rule MF_01631 SAAS SAAS005835
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell morphogenesis

Inferred from electronic annotation. Source: HAMAP

lipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region1 – 230230Pyrophosphorylase By similarity HAMAP-Rule MF_01631
Region9 – 124UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region78 – 792UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region231 – 25121Linker By similarity HAMAP-Rule MF_01631
Region252 – 459208N-acetyltransferase By similarity HAMAP-Rule MF_01631
Region386 – 3872Acetyl-CoA binding By similarity HAMAP-Rule MF_01631

Sites

Active site3631Proton acceptor By similarity HAMAP-Rule MF_01631
Metal binding1031Magnesium By similarity HAMAP-Rule MF_01631
Metal binding2281Magnesium By similarity HAMAP-Rule MF_01631
Binding site231UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site731UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1401UDP-GlcNAc; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site1551UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1701UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site2281UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site3331Acetyl-CoA; amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site3511Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3661Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3771Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4231Acetyl-CoA; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site4401Acetyl-CoA By similarity HAMAP-Rule MF_01631

Sequences

Sequence LengthMass (Da)Tools
E3IID5 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: 1D0C59DCD815BD5A

FASTA45949,326
        10         20         30         40         50         60 
MVKRYAVILA AGQGTRMKSK QYKVLHPVCG KPMVQHVVDQ VLQLGIEKLI TVVGFGAEQV 

        70         80         90        100        110        120 
KMQLGDQSEY AFQQEQLGTA HAVMQAASHL HGKDGVTLVV CGDTPLITAE TMQALLDHHL 

       130        140        150        160        170        180 
ATKAKATVLT AIADNPAGYG RIVRDSHGNV AKIVEHKDAS EQERAIKEIN TGTYCFDNKS 

       190        200        210        220        230        240 
LFEALTHVSN NNVQGEYYLT DVIEILKSNG GIISAYEAPS FEETIGVNDR AALAEAEKIM 

       250        260        270        280        290        300 
RARICRKHML NGVTIIDPAH TYISAEAQIG RDTVIYPGTV IEGKTVIGED CIIGPNSEIK 

       310        320        330        340        350        360 
DCLIGNGTTI RHSVAHDSEI GNDVTIGPFA HIRPLSKIAD EVRIGNFVEV KKSVFGKGSK 

       370        380        390        400        410        420 
ASHLSYIGDA EIGADVNLGC GSITVNYDGK NKHMTKIEDG AFIGCNVNLI APVTVGKGAY 

       430        440        450 
VAAGSTITDD VPANALSIAR ARQVNKENYV DRLSIKKNS

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References

[1]"Complete sequence of chromosome of Geobacillus sp. Y4.1MC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G. expand/collapse author list , Brumm P., Mead D., Woyke T.
Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y4.1MC1 EMBL ADP72902.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002293 Genomic DNA. Translation: ADP72902.1.
RefSeqYP_003987513.1. NC_014650.1.

3D structure databases

ProteinModelPortalE3IID5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP72902; ADP72902; GY4MC1_0046.
GeneID9926864.
KEGGgmc:GY4MC1_0046.
PATRIC42629742. VBIGeoSp111282_0046.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000283476.
KOK04042.
OMAEPQTHLR.

Enzyme and pathway databases

BioCycGSP581103:GHT2-58-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 3 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE3IID5_GEOS0
AccessionPrimary (citable) accession number: E3IID5
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: May 29, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info