ID   GLPB_ECO24              Reviewed;         419 AA.
AC   A7ZP63;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=EcE24377A_2540;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV17511.1; -; Genomic_DNA.
DR   RefSeq; WP_001209926.1; NC_009801.1.
DR   AlphaFoldDB; A7ZP63; -.
DR   KEGG; ecw:EcE24377A_2540; -.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000001122; 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..419
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_1000062191"
SQ   SEQUENCE   419 AA;  45443 MW;  AA766A41D9056AD1 CRC64;
     MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI
     HSGLESLRQQ APAHPYSLLE PQRVLDLACQ AQALIAESGA QLQGSVELAH QRVTPLGTLR
     ATWLSSPEVP VWPLPVKKIC VVGISGLMDF QAHLAAASLR ELDLSVETAE IELPELDVLR
     NNATEFRAVN IARFLDNEEN WPLLLDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP
     CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI
     PLRPRFAVLA SGSFFSGGLV AERNGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV
     TTDETLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ
//