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Reviewed, UniProtKB/Swiss-Prot Q0I239 (GLPB_HAES1)

Last modified June 16, 2009. Version 28. 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: HS_0513
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length432 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 – 432432Anaerobic glycerol-3-phosphate dehydrogenase subunit B HAMAP MF_00753
PRO_1000046606

Sequences

Sequence LengthMass (Da)Tools
Q0I239-1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 65C87F49308B214D

FASTA43248,078
        10         20         30         40         50         60 
MKFDVVIIGG GLAGLTCGIM LQQKGKCCAI INNGQSAMNF SSGSMDLLSQ LPNGEKINSF 

        70         80         90        100        110        120 
EQGYDSLEEQ LPNHPYCLFG KQHVLQKAKQ FEQLIEKINL NVTGSYKQNH FRVTPLGGLH 

       130        140        150        160        170        180 
RTWLSADCIP TMDLHDEHFG YQKITVLGIE GYHDFQPHLL AENLIQHPQF THCSITTALL 

       190        200        210        220        230        240 
HLPELDQLRL TSREFRSVNI SQLLEHRLAF RELVQEIKQA SGDGEAIFLP ACFGLDNQDF 

       250        260        270        280        290        300 
FNKLTLETGL NLYELPTLPP SLVGLRQHKK LKTYFEKLGG FILNGDKALR AVIEDQQVKQ 

       310        320        330        340        350        360 
IYTQLHQEHG IFAEHFVLAS GSFFSNGLVS VFDRLLEPIF DVDMIGNSMI DIQNRLTWTA 

       370        380        390        400        410        420 
RRFSSPQPYQ SAGVAINSCC QLKKSGQIIK NLYAAGNVIG GYNALELGCG SGVAVVTALT 

       430 
VADNIIEAQN RV 

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References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000436 Genomic DNA. Translation: ABI24790.1.
RefSeqYP_718724.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4239995.
GenomeReviewsGene locus HS_0513 in contig CP000436_GR.
KEGGhso:HS_0513.
NMPDRfig|205914.1.peg.1406.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0I239.
OMAQ0I239. TWLSQPF.

Enzyme and pathway databases

BioCycHSOM205914:HS_0513-MON.

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_HAES1
AccessionPrimary (citable) accession number: Q0I239
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: June 16, 2009
This is version 28 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