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   16-JUN-2009, entry version 46.
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=VC_A0748;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1;
RX   MEDLINE=20406833; 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.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   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.
CC       Uses fumarate or nitrate as electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone =
CC       glycerone phosphate + a quinol.
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate
CC       (anaerobic route): step 1/1.
CC   -!- SUBUNIT: Composed of a catalytic glpA/B dimer and of membrane
CC       bound glpC (By similarity).
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family.
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DR   EMBL; AE003853; AAF96646.1; -; Genomic_DNA.
DR   PIR; F82422; F82422.
DR   RefSeq; NP_233134.1; -.
DR   GeneID; 2611901; -.
DR   GenomeReviews; AE003853_GR; VC_A0748.
DR   KEGG; vch:VCA0748; -.
DR   TIGR; VC_A0748; -.
DR   HOGENOM; Q9KLJ6; -.
DR   OMA; Q9KLJ6; TWLSQPF.
DR   BRENDA; 1.1.99.5; 19019.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00753; -; 1.
DR   InterPro; IPR009158; Anaerobic_glycerol3P_DH_bsu.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR   TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Flavoprotein; FMN; Oxidoreductase.
FT   CHAIN         1    436       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit B.
FT                                /FTId=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
//