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Reviewed, UniProtKB/Swiss-Prot A1JIB0 (GLPB_YERE8)

Last modified June 16, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Anaerobic glycerol-3-phosphate dehydrogenase subunit B
      Short name=Anaerobic G-3-P dehydrogenase subunit B
      Short name=Anaerobic G3Pdhase B
    EC=1.1.5.3
Gene names
Name: glpB
Ordered Locus Names: YE0213
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor By similarity.

Catalytic activity

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. HAMAP MF_00753

Cofactor

FMN By similarity.

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. HAMAP MF_00753

Subunit structure

Composed of a catalytic glpA/B dimer and of membrane bound glpC By similarity.

Sequence similarities

Belongs to the anaerobic G-3-P dehydrogenase subunit B family.

Ontologies

Keywords
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

glycerol-3-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Anaerobic glycerol-3-phosphate dehydrogenase subunit B HAMAP MF_00753
PRO_1000046609

Sequences

Sequence LengthMass (Da)Tools
A1JIB0-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0A01C10B657D194D

FASTA42445,149
        10         20         30         40         50         60 
MKFDVIIIGG GLAGLVCGIR LAEQGKYCAI VSAGQNALHF SSGSLDLLAK LPNGQAVSQP 

        70         80         90        100        110        120 
LSALETLAEL APEHPYSKMG QTGQVGELAQ QAESLLSRCG LSLVGSAAKN HLRLTPLGNC 

       130        140        150        160        170        180 
RPTWLSPADI PVAPLEGPLP WQKVAVIGIE GFLDFQPQMV ASALQEQGVE VTSDYLHLPA 

       190        200        210        220        230        240 
LDRLRDNPSE FRAVNIARVL DLPENLQPLA DELARLSSTA EMILLPACIG LDESAPLEAL 

       250        260        270        280        290        300 
RAAVGKPIQL LPTLPPSLLG MRLHQALRHR FQQLGGIVMP GDAVLRAELV GNRITGLYSR 

       310        320        330        340        350        360 
NHGDIPLRAA QMVLASGSFF SNGLVATFEH VYEPILDLDI LSLPNRADWS NSNMFAPQPY 

       370        380        390        400        410        420 
LQFGVNTDNR LRALRGGVAL DNLHVIGAVL GGYDPLQQGC GAGVSLTSAL FVAEQIVSAM 


EVTL 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed: 17173484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM286415 Genomic DNA. Translation: CAL10348.1.
RefSeqYP_001004600.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4715555.
GenomeReviewsGene locus YE0213 in contig AM286415_GR.
KEGGyen:YE0213.
NMPDRfig|630.2.peg.208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA1JIB0. TWLSQPF.

Family and domain databases

HAMAPMF_00753.
[Tree]
InterProIPR009158. Anaerobic_glycerol3P_DH_bsu.
IPR003953. FAD_bind2_N.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000141. Anaerobic_G3P_dh. 1 hit.
TIGRFAMsTIGR03378. glycerol3P_GlpB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLPB_YERE8
AccessionPrimary (citable) accession number: A1JIB0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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) · Sequences · References · Cross-references · Entry information · Relevant documents