ID   GLPB_SALTY              Reviewed;         419 AA.
AC   Q8ZNG4;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 123.
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};
GN   OrderedLocusNames=STM2285;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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 = 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   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC       Note=Loosely bound to the cytoplasmic membrane often occurring in
CC       vesicles associated with fumarate reductase. {ECO:0000250}.
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; AE006468; AAL21186.1; -; Genomic_DNA.
DR   RefSeq; NP_461227.1; NC_003197.2.
DR   RefSeq; WP_000667146.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZNG4; -.
DR   STRING; 99287.STM2285; -.
DR   PaxDb; 99287-STM2285; -.
DR   GeneID; 1253807; -.
DR   KEGG; stm:STM2285; -.
DR   PATRIC; fig|99287.12.peg.2418; -.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OMA; CFGLENQ; -.
DR   PhylomeDB; Q8ZNG4; -.
DR   BioCyc; SENT99287:STM2285-MONOMER; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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   Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..419
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000204566"
SQ   SEQUENCE   419 AA;  45671 MW;  32450A4C51504778 CRC64;
     MKFDTVIMGG GLAGLLCGLQ LQQHGLRCAI VTRGQSALHF SSGSLDLLSA LPDGQPVTDI
     TAGLDALCRQ APEHPYSRLG AQKVLTLAQQ AQTLLNASGA QLYGDVQQAH QRVTPLGTLR
     STWLSSPEVP VWPLSAQRIC VVGVSGLLDF QAHLAAASLR QRDLNVETAE IDLPELDVLR
     DNPTEFRAVN IARLLDNEEK WPLLYDALSP IATNCDMIIM PACFGLANDT LWRWLNERLP
     CALTLLPTLP PSVLGIRLHN QLQRQFVRQG GIWMPGDEVK KVTCRRGTVS EIWTRNHADI
     PLRPRFAVLA SGSFFSSGLV AEREGIREPI LGLDVQQTAT RAEWYQQHFF DPQPWQQFGV
     VTDDAFRPSL AGNTVENLYA IGSVLAGFDP IAEGCGGGVC AVSALQAAHH IAERAGEQQ
//