ID   GLPB_PASMU              Reviewed;         428 AA.
AC   Q9CL07;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   18-JUN-2025, entry version 126.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G3Pdhase B {ECO:0000255|HAMAP-Rule:MF_00753};
DE            EC=1.1.5.3 {ECO:0000255|HAMAP-Rule:MF_00753};
GN   Name=glpB {ECO:0000255|HAMAP-Rule:MF_00753}; OrderedLocusNames=PM1441;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC       fumarate or nitrate as electron acceptor. {ECO:0000255|HAMAP-
CC       Rule:MF_00753}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + a quinol; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00753};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00753};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK03525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004439; AAK03525.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005724104.1; NC_002663.1.
DR   AlphaFoldDB; Q9CL07; -.
DR   STRING; 272843.PM1441; -.
DR   EnsemblBacteria; AAK03525; AAK03525; PM1441.
DR   KEGG; pmu:PM1441; -.
DR   PATRIC; fig|272843.6.peg.1455; -.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OrthoDB; 6395323at2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase (FAD) complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019563; P:glycerol catabolic 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-dep_OxRdtase_2_FAD-bd.
DR   InterPro; IPR050315; FAD-oxidoreductase_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009158; G3P_DH_GlpB_su.
DR   NCBIfam; TIGR03378; glycerol3P_GlpB; 1.
DR   NCBIfam; NF003718; PRK05329.1-1; 1.
DR   NCBIfam; NF003719; PRK05329.1-2; 1.
DR   NCBIfam; NF003720; PRK05329.1-3; 1.
DR   NCBIfam; NF003721; PRK05329.1-4; 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..428
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000204564"
SQ   SEQUENCE   428 AA;  47374 MW;  417C12050CA54C17 CRC64;
     MNFDVVIIGG GLAGLTCGIA LQTQGKQCVI INNGQAAIDF SSGSLDLLGQ LPSGRQIQHF
     EQNYTALYQQ AAQHPYALVG KDKVIEKARQ FEQLAQTLNL GLVGTCDKNH FRVTPLGGLR
     PTWLSPNSVP IVTNEEMFPH RKIAVLGIEG YHDFQPQLLA ENLVQHAQFA HCEVTTGYLN
     IPELDHLRHQ SREFRSVNIA QLLEHKLAFS DLVREIREAV NGASAVFLPA CFGLETQEFF
     SALKQATQLE LFELPTLPPS LLGMRQHKQL TQHFKQLGGL MMNGDKVIAA DVHHQRVTQV
     YTQLHQEIPI QAKDVVLASG SFFSKGLVAE FEKIREPIFA LDLVENDRFN LQDRMTWTHS
     RFSAPQPYQQ TGVVIDEHCR ARKSGQFFEN LYAIGNIVGG FNGIELGCGS GVAIVTALVA
     AEQIGGEK
//