GLPB_ECOLI
ID GLPB_ECOLI Reviewed; 419 AA.
AC P13033;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B;
DE Short=Anaerobic G-3-P dehydrogenase subunit B;
DE Short=Anaerobic G3Pdhase B;
DE EC=1.1.5.3;
GN Name=glpB; OrderedLocusNames=b2242, JW2236;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=3286606; DOI=10.1128/jb.170.6.2448-2456.1988;
RA Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F.,
RA Weiner J.H.;
RT "Nucleotide sequence and gene-polypeptide relationships of the glpABC
RT operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of
RT Escherichia coli K-12.";
RL J. Bacteriol. 170:2448-2456(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC fumarate or nitrate as electron acceptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC Note=Loosely bound to the cytoplasmic membrane often occurring in
CC vesicles associated with fumarate reductase.
CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC family. {ECO:0000305}.
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DR EMBL; M20938; AAA83865.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75302.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16061.1; -; Genomic_DNA.
DR PIR; B32006; DEECNB.
DR RefSeq; NP_416745.1; NC_000913.3.
DR RefSeq; WP_001209927.1; NZ_LN832404.1.
DR AlphaFoldDB; P13033; -.
DR BioGRID; 4260490; 447.
DR BioGRID; 851074; 1.
DR ComplexPortal; CPX-4841; Anaerobic glycerol-3-phosphate dehydrogenase complex.
DR DIP; DIP-9791N; -.
DR IntAct; P13033; 5.
DR STRING; 511145.b2242; -.
DR PaxDb; P13033; -.
DR PRIDE; P13033; -.
DR EnsemblBacteria; AAC75302; AAC75302; b2242.
DR EnsemblBacteria; BAA16061; BAA16061; BAA16061.
DR GeneID; 946733; -.
DR KEGG; ecj:JW2236; -.
DR KEGG; eco:b2242; -.
DR PATRIC; fig|511145.12.peg.2331; -.
DR EchoBASE; EB0387; -.
DR eggNOG; COG3075; Bacteria.
DR HOGENOM; CLU_047793_0_0_6; -.
DR InParanoid; P13033; -.
DR OMA; CFGLENQ; -.
DR PhylomeDB; P13033; -.
DR BioCyc; EcoCyc:ANGLYC3PDEHYDROGSUBUNITB-MON; -.
DR BioCyc; MetaCyc:ANGLYC3PDEHYDROGSUBUNITB-MON; -.
DR UniPathway; UPA00618; UER00673.
DR PRO; PR:P13033; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; ISM:EcoCyc.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IDA:EcoCyc.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00753; Glycerol3P_GlpB; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009158; G3P_DH_GlpB_su.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Flavoprotein; FMN; Membrane; Oxidoreductase; Reference proteome.
FT CHAIN 1..419
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT B"
FT /id="PRO_0000204559"
SQ SEQUENCE 419 AA; 45357 MW; C8A2285AD09F4F55 CRC64;
MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI
HSGLESLRQQ APAHPYSLLE PQRVLDLACQ AQALIAESGA QLQGSVELAH QRVTPLGTLR
STWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELGLAVETAE IELPELDVLR
NNATEFRAVN IARFLDNEEN WPLLLDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP
CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI
PLRPRFAVLA SGSFFSGGLV AERNGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV
TTDETLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ
