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GLPB_VIBCH
ID   GLPB_VIBCH              Reviewed;         436 AA.
AC   Q9KLJ6;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G3Pdhase B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            EC=1.1.5.3 {ECO:0000255|HAMAP-Rule:MF_00753};
GN   Name=glpB {ECO:0000255|HAMAP-Rule:MF_00753}; OrderedLocusNames=VC_A0748;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC       fumarate or nitrate as electron acceptor. {ECO:0000255|HAMAP-
CC       Rule:MF_00753}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00753};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00753};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family. {ECO:0000255|HAMAP-Rule:MF_00753}.
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DR   EMBL; AE003853; AAF96646.1; -; Genomic_DNA.
DR   PIR; F82422; F82422.
DR   RefSeq; NP_233134.1; NC_002506.1.
DR   RefSeq; WP_000972312.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KLJ6; -.
DR   STRING; 243277.VC_A0748; -.
DR   DNASU; 2611901; -.
DR   EnsemblBacteria; AAF96646; AAF96646; VC_A0748.
DR   KEGG; vch:VC_A0748; -.
DR   PATRIC; fig|243277.26.peg.3375; -.
DR   eggNOG; COG3075; Bacteria.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OMA; CFGLENQ; -.
DR   BioCyc; VCHO:VCA0748-MON; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase; Reference proteome.
FT   CHAIN           1..436
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000204568"
SQ   SEQUENCE   436 AA;  48019 MW;  EDB2B15CFF0CEC7B CRC64;
     MMHYDVAVIG GGIAGYSAAL RALQAGKKVV LINQGQSALH FSSGSIDVLG RLPDGSVVNQ
     PFDALSALQQ QAPEHPYSKV GRKNSEKGLM WFKRTLDSAH VPLHHEPDGA NHWRITPLGT
     LKNTWLSQPF VYPYRGNADF SRIMIVAIDG YRDFQPAMLR DNLAQRPELA NTPMLTVNVS
     IPGFEGFRRN PNELRSIDIA RLLRQESAWN ALCDQLMRVA RPDDLVIMPA IMGNGDGLHL
     MSKLQQVTQL RFHEVPTMPP SLLGIRIEEA LHRSFIQGGG VQLKGDKVIG GNFAGSRLTA
     IHTQNLRDFP ISAEHYVMAT GSYFSQGLQA SQHAIQEPIF ALDVQQNPDR AQWRHAQFIA
     AQSHPFMTFG VTTDANLHPS RQGKTIDNLW CCGAMLSGYD PVFEGCGGGV AIATAYHAVE
     QILATYAQTK QPEVLL
 
 
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