ID   GLPB_ECOL6              Reviewed;         419 AA.
AC   Q8FFN4;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
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=c2783;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein (By similarity). Note=Loosely bound to the cytoplasmic
CC       membrane often occurring in vesicles associated with fumarate
CC       reductase (By similarity).
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE014075; AAN81237.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_754669.1; -.
DR   GeneID; 1038299; -.
DR   GenomeReviews; AE014075_GR; c2783.
DR   KEGG; ecc:c2783; -.
DR   NMPDR; fig|199310.1.peg.2712; -.
DR   HOGENOM; Q8FFN4; -.
DR   OMA; Q8FFN4; TWLSQPF.
DR   BRENDA; 1.1.99.5; 292881.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein;
KW   FMN; Membrane; Oxidoreductase.
FT   CHAIN         1    419       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit B.
FT                                /FTId=PRO_0000204560.
SQ   SEQUENCE   419 AA;  45398 MW;  21E116E3644E0EDD CRC64;
     MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI
     HSGLESLRQQ APAHPYTLLG PQRVLDLACQ AQALIAESGA QLQGSVELAH QRITPLGTLR
     STWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELDLAVETAE IELPELDVLR
     NNATEFRAVN IARFLDNEEN WPLIIDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP
     CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI
     PLRPRFVVLA SGSFFSGGLV AERDGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV
     TTDEALRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHVAQQ IAQRAGGQQ
//