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GLPB_PECAS
ID   GLPB_PECAS              Reviewed;         420 AA.
AC   Q6CZI7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=ECA4164;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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;
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; BX950851; CAG77061.1; -; Genomic_DNA.
DR   RefSeq; WP_011095635.1; NC_004547.2.
DR   AlphaFoldDB; Q6CZI7; -.
DR   STRING; 218491.ECA4164; -.
DR   EnsemblBacteria; CAG77061; CAG77061; ECA4164.
DR   KEGG; eca:ECA4164; -.
DR   PATRIC; fig|218491.5.peg.4236; -.
DR   eggNOG; COG3075; Bacteria.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OMA; CFGLENQ; -.
DR   OrthoDB; 1152849at2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000007966; 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; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT                   B"
FT                   /id="PRO_0000258899"
SQ   SEQUENCE   420 AA;  45223 MW;  44703F417A72903E CRC64;
     MRYDVVIIGG GLAGLTCGIR LAEQGKRCAI VSAGQNALHF SSGALDLLSH LPDGQPVSQP
     LDALDELARQ APHHPYSRMG AAAVAALLPQ VEALLERSNI SLLGNHQQNH WRMTPLGKFR
     ACWLSPADGV TRGLADSHFG DNPLIAGIEG FLDFQSRIVA GTLQTQGIAA RSDELKLPVL
     DRLRQNPSEF RAVNIARLLD RPENRSALVE ELSLLANGND AIIMPACLGL DSPEIVSELA
     DALGKPVLLL PTLPPSVLGL RLHQALSQRF RQLGGMVMPG DRAVRASLSS QEIAVHSHHH
     RDIPLRAKHA VLASGSFFSN GLVTQFDRVT EPVFGLDVRF AEQREGWSQQ DVFAPQPYMQ
     FGAIVDEHLH PRIAGETVNN LYAIGAVLEG FDPIVQGCGA GVSLLSALHV AEQILKEGNP
 
 
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