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Protein

Anaerobic glycerol-3-phosphate dehydrogenase subunit B

Gene

glpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.

Catalytic activityi

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

Cofactori

Pathwayi

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase activity Source: EcoCyc
  2. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycerol-3-phosphate metabolic process Source: UniProtKB-HAMAP
  2. glycerol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciEcoCyc:ANGLYC3PDEHYDROGSUBUNITB-MONOMER.
ECOL316407:JW2236-MONOMER.
MetaCyc:ANGLYC3PDEHYDROGSUBUNITB-MONOMER.
UniPathwayiUPA00618; UER00673.

Names & Taxonomyi

Protein namesi
Recommended name:
Anaerobic glycerol-3-phosphate dehydrogenase subunit B (EC:1.1.5.3)
Short name:
Anaerobic G-3-P dehydrogenase subunit B
Short name:
Anaerobic G3Pdhase B
Gene namesi
Name:glpB
Ordered Locus Names:b2242, JW2236
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10392. glpB.

Subcellular locationi

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

GO - Cellular componenti

  1. plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Anaerobic glycerol-3-phosphate dehydrogenase subunit BPRO_0000204559Add
BLAST

Proteomic databases

PaxDbiP13033.
PRIDEiP13033.

Expressioni

Gene expression databases

GenevestigatoriP13033.

Interactioni

Subunit structurei

Composed of a catalytic GlpA/B dimer and of membrane bound GlpC.

Protein-protein interaction databases

DIPiDIP-9791N.
IntActiP13033. 5 interactions.
MINTiMINT-1319997.
STRINGi511145.b2242.

Structurei

3D structure databases

ProteinModelPortaliP13033.
SMRiP13033. Positions 3-51.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3075.
HOGENOMiHOG000278489.
InParanoidiP13033.
KOiK00112.
OMAiWYQRDFF.
OrthoDBiEOG6K6V62.
PhylomeDBiP13033.

Family and domain databases

HAMAPiMF_00753. Glycerol3P_GlpB.
InterProiIPR003953. FAD_bind_dom.
IPR009158. G3P_DH_GlpB_su.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000141. Anaerobic_G3P_dh. 1 hit.
TIGRFAMsiTIGR03378. glycerol3P_GlpB. 1 hit.

Sequencei

Sequence statusi: Complete.

P13033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH
60 70 80 90 100
LPDGQPVTDI HSGLESLRQQ APAHPYSLLE PQRVLDLACQ AQALIAESGA
110 120 130 140 150
QLQGSVELAH QRVTPLGTLR STWLSSPEVP VWPLPAKKIC VVGISGLMDF
160 170 180 190 200
QAHLAAASLR ELGLAVETAE IELPELDVLR NNATEFRAVN IARFLDNEEN
210 220 230 240 250
WPLLLDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP CSLMLLPTLP
260 270 280 290 300
PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI
310 320 330 340 350
PLRPRFAVLA SGSFFSGGLV AERNGIREPI LGLDVLQTAT RGEWYKGDFF
360 370 380 390 400
APQPWQQFGV TTDETLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC
410
AVSALHAAQQ IAQRAGGQQ
Length:419
Mass (Da):45,357
Last modified:January 1, 1990 - v1
Checksum:iC8A2285AD09F4F55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20938 Genomic DNA. Translation: AAA83865.1.
U00096 Genomic DNA. Translation: AAC75302.1.
AP009048 Genomic DNA. Translation: BAA16061.1.
PIRiB32006. DEECNB.
RefSeqiNP_416745.1. NC_000913.3.
YP_490481.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75302; AAC75302; b2242.
BAA16061; BAA16061; BAA16061.
GeneIDi12931496.
946733.
KEGGiecj:Y75_p2204.
eco:b2242.
PATRICi32119843. VBIEscCol129921_2331.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20938 Genomic DNA. Translation: AAA83865.1.
U00096 Genomic DNA. Translation: AAC75302.1.
AP009048 Genomic DNA. Translation: BAA16061.1.
PIRiB32006. DEECNB.
RefSeqiNP_416745.1. NC_000913.3.
YP_490481.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP13033.
SMRiP13033. Positions 3-51.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9791N.
IntActiP13033. 5 interactions.
MINTiMINT-1319997.
STRINGi511145.b2242.

Proteomic databases

PaxDbiP13033.
PRIDEiP13033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75302; AAC75302; b2242.
BAA16061; BAA16061; BAA16061.
GeneIDi12931496.
946733.
KEGGiecj:Y75_p2204.
eco:b2242.
PATRICi32119843. VBIEscCol129921_2331.

Organism-specific databases

EchoBASEiEB0387.
EcoGeneiEG10392. glpB.

Phylogenomic databases

eggNOGiCOG3075.
HOGENOMiHOG000278489.
InParanoidiP13033.
KOiK00112.
OMAiWYQRDFF.
OrthoDBiEOG6K6V62.
PhylomeDBiP13033.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00673.
BioCyciEcoCyc:ANGLYC3PDEHYDROGSUBUNITB-MONOMER.
ECOL316407:JW2236-MONOMER.
MetaCyc:ANGLYC3PDEHYDROGSUBUNITB-MONOMER.

Miscellaneous databases

PROiP13033.

Gene expression databases

GenevestigatoriP13033.

Family and domain databases

HAMAPiMF_00753. Glycerol3P_GlpB.
InterProiIPR003953. FAD_bind_dom.
IPR009158. G3P_DH_GlpB_su.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000141. Anaerobic_G3P_dh. 1 hit.
TIGRFAMsiTIGR03378. glycerol3P_GlpB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12."
    Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F., Weiner J.H.
    J. Bacteriol. 170:2448-2456(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiGLPB_ECOLI
AccessioniPrimary (citable) accession number: P13033
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 4, 2015
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.