ID   GLPB_MANSM              Reviewed;         431 AA.
AC   Q65R09;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=MS1994;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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 = 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         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}.
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DR   EMBL; AE016827; AAU38601.1; -; Genomic_DNA.
DR   RefSeq; WP_011201152.1; NC_006300.1.
DR   AlphaFoldDB; Q65R09; -.
DR   STRING; 221988.MS1994; -.
DR   KEGG; msu:MS1994; -.
DR   eggNOG; COG3075; Bacteria.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OrthoDB; 6395323at2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000607; 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.
FT   CHAIN           1..431
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000258903"
SQ   SEQUENCE   431 AA;  47213 MW;  6C56478C9A41F3CA CRC64;
     MNFDVVIIGA GIAGLTCGLT LQEKGVRCAI INNGQAALDF SSGSMDLLSR LPNGSTVDSF
     AQSYAALAQQ SPNHPYVILG KDVVLDKIQQ FETLAKSLNL SLVGSSDKNH KRVTALGGLR
     GTWLSPNSVP TVSLEGKFPH DNIVLLGIEG YHDFQPQLLA DNLKQNPQFA HCEITTNFLH
     IPELDHLRQN SREFRSVNIA QVLEYKLSFN NLVDEIKQAV GNAKAAFLPA CFGLDDQSFF
     ESLKQATGIE LYELPTLPPS LLGIRQHRQL RHRFEKLGGV MFNGDRALRS EFEGNKVARI
     FTQLHLENAV TAKYFVLASG GFFSNGLVSE FEEIYEPLFR SDIVKTERFN ATDRFSWISK
     RFADPQPYQS AGVVINAECQ VQKDGNNVEN LFAIGAVIGG YNGIELGCGS GVAVTTALKV
     ADNIIAKESS N
//