GLPB_PECCP
ID GLPB_PECCP Reviewed; 420 AA.
AC C6DH98;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=PC1_3956;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000255|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: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; CP001657; ACT14971.1; -; Genomic_DNA.
DR RefSeq; WP_015842052.1; NC_012917.1.
DR AlphaFoldDB; C6DH98; -.
DR STRING; 561230.PC1_3956; -.
DR EnsemblBacteria; ACT14971; ACT14971; PC1_3956.
DR KEGG; pct:PC1_3956; -.
DR eggNOG; COG3075; Bacteria.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OMA; CFGLENQ; -.
DR OrthoDB; 1152849at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000002736; Chromosome.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
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; -; 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 Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..420
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT B"
FT /id="PRO_1000212851"
SQ SEQUENCE 420 AA; 45149 MW; 88CF5FAEF0BBCE9D CRC64;
MRYDVVIIGG GLAGLTCGIR LAEQGKRCAI VSAGQNALHF SSGALDLLSH LPDGQPVSQP
LEALDELARQ APHHPYSRMG AAAVAALLPQ VEALLERSTI SLLGSYQQNH WRMTPLGKFR
ACWLSPVDGV TRGLPDSRFG DNPLIAGIEG FLDFQSRIVA GTLQAQGIAA RSDDLKLPVL
DRLRQNPSEF RAVNIARVLD RPENRAALVE ELSLLANGND AIIMPACLGL DSPEVVGELA
EALGKPISLL PTLPPSVLGL RLHQALSQRF RQLGGMVMPG DRAVRASLSA QEIAVHSHHH
RDIPLRAKYA VLASGSFFSN GLVTQFDRVT EPVFGLDVRF AEQREGWSQQ DVFVPQPYMQ
FGAIVDEHLH PRIGGETIGN LYAIGAVLEG FDPIAQGCGA GVSLLSALHV AEQILKEGNL