ID   GLPB_PHOPR              Reviewed;         442 AA.
AC   Q6LSE4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=PBPRA1371;
OS   Photobacterium profundum (Photobacterium sp. (strain SS9)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=74109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
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.
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; CR378667; CAG19782.1; -; Genomic_DNA.
DR   RefSeq; YP_129584.1; -.
DR   GeneID; 3122523; -.
DR   GenomeReviews; CR354531_GR; PBPRA1371.
DR   KEGG; ppr:PBPRA1371; -.
DR   NMPDR; fig|298386.1.peg.3625; -.
DR   HOGENOM; Q6LSE4; -.
DR   OMA; Q6LSE4; TWLSQPF.
DR   BioCyc; PPRO298386:PBPRA1371-MON; -.
DR   BRENDA; 1.1.99.5; 263915.
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    442       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit B.
FT                                /FTId=PRO_0000258904.
SQ   SEQUENCE   442 AA;  48789 MW;  4B3CB72D1B484C57 CRC64;
     MKFDSLIIGG GVAGLSCAIR CAEAGMKTAV IAAGQSALHF SSGSIDFLSR LPNGQPVYHP
     MAAFNELQQQ SPEHPYCKLG KRKVQEALDW YQEMIKARGI YLSSQEDEAN HLRLTPMGTF
     RSTWLSQQTV HQFPLTNTAG ELNHIALVTV DGFRDFQPKL AADNLSKLAQ FKDVKITTAA
     VELPDFEEMQ RNPCEFRSID ISRVLRDERK LHAFAKSMIQ AVGKADLVVL PAVFGNGDGA
     ATIKLLEGLT GFTICELPTM PPSLLGIRLE EAMKSHFKML GGIILVGDEV QRGDIEDGEL
     KRIFTRNHRD MPLIADNYLI ATGSFFSRGM AAQRLSIDEP IFNLDTVAIP DRDQWYQPEF
     FASKAHPFLK MGVICNDQLQ ASANNQTIDN LFCAGALLAH YDPVFEGCGS GVAISTGFHV
     AEQMISKHTA RQNQNNKERT IA
//