ID   GLPB_HAEIN              Reviewed;         432 AA.
AC   P43800;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 136.
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=HI_0684;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC       fumarate or nitrate as electron acceptor (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22344.1; -; Genomic_DNA.
DR   RefSeq; NP_438844.1; NC_000907.1.
DR   AlphaFoldDB; P43800; -.
DR   STRING; 71421.HI_0684; -.
DR   DNASU; 950690; -.
DR   EnsemblBacteria; AAC22344; AAC22344; HI_0684.
DR   KEGG; hin:HI_0684; -.
DR   PATRIC; fig|71421.8.peg.715; -.
DR   eggNOG; COG3075; Bacteria.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OrthoDB; 6395323at2; -.
DR   PhylomeDB; P43800; -.
DR   BioCyc; HINF71421:G1GJ1-719-MONOMER; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
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; FAD/NAD(P)-binding domain; 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   NCBIfam; TIGR03378; glycerol3P_GlpB; 1.
DR   PANTHER; PTHR43400:SF11; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase; Reference proteome.
FT   CHAIN           1..432
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000204563"
SQ   SEQUENCE   432 AA;  47251 MW;  6D99EEAC75549228 CRC64;
     MNFDVAIIGG GLAGLTCAIA LQQRGKRCVI INNGQAAIDF ASGSLDLLSR MPSTTYGENR
     AVENLKENIT ALRNELPAHP YSLLGAEKVL AKAQDFERLA NELHLDLIGS TEKNHWRVTG
     LGSLRGAWLS PNSVPTVQGN EPFPHKRIAV LGIEGYHDFQ PQLLAANLVL NPQFEHCEVT
     SGFLNIPQLD ELRKNAREFR SVNISQLLEH KLAFKDLVKE IIESAQGAEA VFLPACFGLE
     NQEFMTALRD ATKLALFELP TLPPSLLGMR QRIQLRHKFE SLGGLMINGD SALNATFEGN
     QVRCINTRLL EDEEITADNF VLASGSFFSK GLISEFDKIY EPVFESDIIG VEGFNNKDRF
     TWTAHRFAHP QPYQSAGVAI NAQCQVKKCG QFLTNLYAVG NVIGGFNALE LGCGSGVAVV
     TALAVADEIL AK
//