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Reviewed, UniProtKB/Swiss-Prot Q8FFN4 (GLPB_ECOL6)

Last modified June 16, 2009. Version 46. 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: c2783
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length419 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.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity. Note: Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 419419Anaerobic glycerol-3-phosphate dehydrogenase subunit B HAMAP MF_00753
PRO_0000204560

Sequences

Sequence LengthMass (Da)Tools
Q8FFN4-1 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: 21E116E3644E0EDD

FASTA41945,398
        10         20         30         40         50         60 
MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI 

        70         80         90        100        110        120 
HSGLESLRQQ APAHPYTLLG PQRVLDLACQ AQALIAESGA QLQGSVELAH QRITPLGTLR 

       130        140        150        160        170        180 
STWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELDLAVETAE IELPELDVLR 

       190        200        210        220        230        240 
NNATEFRAVN IARFLDNEEN WPLIIDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP 

       250        260        270        280        290        300 
CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI 

       310        320        330        340        350        360 
PLRPRFVVLA SGSFFSGGLV AERDGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV 

       370        380        390        400        410 
TTDEALRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHVAQQ IAQRAGGQQ 

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References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

AE014075 Genomic DNA. Translation: AAN81237.1. Different initiation.
RefSeqNP_754669.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1038299.
GenomeReviewsGene locus c2783 in contig AE014075_GR.
KEGGecc:c2783.
NMPDRfig|199310.1.peg.2712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FFN4.
OMAQ8FFN4. TWLSQPF.

Enzyme and pathway databases

BRENDA1.1.99.5. 292881.

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_ECOL6
AccessionPrimary (citable) accession number: Q8FFN4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: June 16, 2009
This is version 46 of the entry and version 2 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