Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7ZP63 (GLPB_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:EcE24377A_2540
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor By similarity. HAMAP-Rule MF_00753

Catalytic activity

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

Cofactor

FMN By similarity. HAMAP-Rule MF_00753

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1. HAMAP-Rule 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
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycerol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionsn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Anaerobic glycerol-3-phosphate dehydrogenase subunit B HAMAP-Rule MF_00753
PRO_1000062191

Sequences

Sequence LengthMass (Da)Tools
A7ZP63 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: AA766A41D9056AD1

FASTA41945,443
        10         20         30         40         50         60 
MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI 

        70         80         90        100        110        120 
HSGLESLRQQ APAHPYSLLE PQRVLDLACQ AQALIAESGA QLQGSVELAH QRVTPLGTLR 

       130        140        150        160        170        180 
ATWLSSPEVP VWPLPVKKIC VVGISGLMDF QAHLAAASLR ELDLSVETAE IELPELDVLR 

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

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

       310        320        330        340        350        360 
PLRPRFAVLA SGSFFSGGLV AERNGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV 

       370        380        390        400        410 
TTDETLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV17511.1.
RefSeqYP_001463592.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZP63.
SMRA7ZP63. Positions 1-60, 257-313, 355-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_2540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV17511; ABV17511; EcE24377A_2540.
GeneID5586856.
KEGGecw:EcE24377A_2540.
PATRIC18294358. VBIEscCol31211_2821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3075.
HOGENOMHOG000278489.
KOK00112.
OMAFRSVNIS.
OrthoDBEOG6K6V62.

Enzyme and pathway databases

BioCycECOL331111:GH7P-2522-MONOMER.
UniPathwayUPA00618; UER00673.

Family and domain databases

HAMAPMF_00753. Glycerol3P_GlpB.
InterProIPR003953. FAD_bind_dom.
IPR009158. G3P_DH_GlpB_su.
[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_ECO24
AccessionPrimary (citable) accession number: A7ZP63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways