ID   GLPB_HAES1              Reviewed;         432 AA.
AC   Q0I239;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=HS_0513;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17172329; DOI=10.1128/JB.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni)
RT   strain 129Pt and comparison to Haemophilus ducreyi 35000HP and
RT   Haemophilus influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI24790.1; -; Genomic_DNA.
DR   RefSeq; YP_718724.1; -.
DR   GeneID; 4239995; -.
DR   GenomeReviews; CP000436_GR; HS_0513.
DR   KEGG; hso:HS_0513; -.
DR   NMPDR; fig|205914.1.peg.1406; -.
DR   HOGENOM; Q0I239; -.
DR   OMA; Q0I239; TWLSQPF.
DR   BioCyc; HSOM205914:HS_0513-MON; -.
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    432       Anaerobic glycerol-3-phosphate
FT                                dehydrogenase subunit B.
FT                                /FTId=PRO_1000046606.
SQ   SEQUENCE   432 AA;  48078 MW;  65C87F49308B214D CRC64;
     MKFDVVIIGG GLAGLTCGIM LQQKGKCCAI INNGQSAMNF SSGSMDLLSQ LPNGEKINSF
     EQGYDSLEEQ LPNHPYCLFG KQHVLQKAKQ FEQLIEKINL NVTGSYKQNH FRVTPLGGLH
     RTWLSADCIP TMDLHDEHFG YQKITVLGIE GYHDFQPHLL AENLIQHPQF THCSITTALL
     HLPELDQLRL TSREFRSVNI SQLLEHRLAF RELVQEIKQA SGDGEAIFLP ACFGLDNQDF
     FNKLTLETGL NLYELPTLPP SLVGLRQHKK LKTYFEKLGG FILNGDKALR AVIEDQQVKQ
     IYTQLHQEHG IFAEHFVLAS GSFFSNGLVS VFDRLLEPIF DVDMIGNSMI DIQNRLTWTA
     RRFSSPQPYQ SAGVAINSCC QLKKSGQIIK NLYAAGNVIG GYNALELGCG SGVAVVTALT
     VADNIIEAQN RV
//