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Q32DU5 (GLPB_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SDY_2437
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella ›

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
Reference 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_0000258908

Sequences

Sequence LengthMass (Da)Tools
Q32DU5 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: D0B172214645EE48

FASTA41945,423
        10         20         30         40         50         60 
MRFDTVIMGG GLAGLLCGLQ LQKHGLRSAI VTRGQSALHF SSGSLDLLSH LPDGQAVTDI 

        70         80         90        100        110        120 
HSGLESLRQQ APAHPYSLLG PQRVLDLACQ AQALIAKSGA QLQGSVELPH QRITPLGTLR 

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

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

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

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

       370        380        390        400        410 
TTDQTLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000034 Genomic DNA. Translation: ABB62510.1.
RefSeqYP_404001.1. NC_007606.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300267.SDY_2437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB62510; ABB62510; SDY_2437.
GeneID3798238.
KEGGsdy:SDY_2437.
PATRIC18695023. VBIShiDys99784_2936.

Phylogenomic databases

eggNOGCOG3075.
HOGENOMHOG000278489.
KOK00112.
OMAFRSVNIS.
OrthoDBEOG6K6V62.
ProtClustDBPRK05329.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-2433-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_SHIDS
AccessionPrimary (citable) accession number: Q32DU5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 64 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

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