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Q1R9H5 (GLPB_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:UTI89_C2522
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [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.

Sequence caution

The sequence ABE07989.1 differs from that shown. Reason: Erroneous initiation.

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_0000258900

Sequences

Sequence LengthMass (Da)Tools
Q1R9H5 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 4FC59D8EC01E7A4F

FASTA41945,342
        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 
PLRPRFAVLA SGSFFSGGLV AERDGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV 

       370        380        390        400        410 
TTDEALRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE07989.1. Different initiation.
RefSeqYP_541520.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R9H5.
SMRQ1R9H5. Positions 1-60, 255-312, 355-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING364106.UTI89_C2522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE07989; ABE07989; UTI89_C2522.
GeneID3992364.
KEGGeci:UTI89_C2522.
PATRIC18454626. VBIEscCol42261_2550.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3075.
HOGENOMHOG000278489.
KOK00112.
OMAFRSVNIS.
OrthoDBEOG6K6V62.

Enzyme and pathway databases

BioCycECOL364106:GHPQ-2504-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_ECOUT
AccessionPrimary (citable) accession number: Q1R9H5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 14, 2014
This is version 59 of the entry and version 2 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