ID A0A0W8JBN1_9VIBR Unreviewed; 446 AA.
AC A0A0W8JBN1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G3Pdhase B {ECO:0000256|HAMAP-Rule:MF_00753};
DE EC=1.1.5.3 {ECO:0000256|HAMAP-Rule:MF_00753};
GN Name=glpB {ECO:0000256|HAMAP-Rule:MF_00753};
GN ORFNames=VRK_32210 {ECO:0000313|EMBL:KUI97658.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI97658.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUI97658.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI97658.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC fumarate or nitrate as electron acceptor. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00753};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00753}.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC family. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUI97658.1}.
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DR EMBL; LQIY01000024; KUI97658.1; -; Genomic_DNA.
DR RefSeq; WP_059122157.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JBN1; -.
DR STRING; 1761910.VRK_32210; -.
DR PATRIC; fig|1761910.3.peg.3254; -.
DR OrthoDB; 6395323at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000054473; Unassembled WGS sequence.
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; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00753};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00753};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00753}.
FT DOMAIN 5..419
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 446 AA; 49006 MW; D1CA18CFAF2E002D CRC64;
MMDYDIAVIG GGIAGYSAAI RSQQAGKKTV LISQGQSALH FSSGSIDVLG RLPTGERVED
PFAAILQLQQ HQFGSSALPG QTDLHPYVKV GRSVVEQSLL WFKEMLAAEI QLSHQPDYAN
HWRITPFGTL KATWLSQPYV YQHRSQASFR EIVIVALAGY RDFQPQILKD NLARVADFAG
IPIRIATIRL PSVAHDQRHP CERRSLDIAH SLQQASVWSS FCEQLTRMTC ADDLVILPAV
VGHGGGMTTL AQLQQATQRY FHEVPTMPPS LMGIRLEAAL HRIFIQAGGI HLKGDQVLGG
HFEGHRLTEV YTRNLTDIPV RAGHYIMATG SYFSQGLQAS RQAIKEPVFG LDVAQMTPRT
QWGTHDFIAD QPHPFMTFGV STDAHLHPSY RGQRIDNLYC CGAMLAGYDP VFEGSGGGVA
IATAYHAIEQ CMGHHVCPAT CQEALS
//