GLPB_YERPE
ID GLPB_YERPE Reviewed; 424 AA.
AC Q8ZAH6; Q0WAI5; Q8CWI2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
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=YPO3825, y0405, YP_3223;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM83994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS63391.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL22412.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83994.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS63391.1; ALT_INIT; Genomic_DNA.
DR PIR; AI0465; AI0465.
DR RefSeq; WP_002211492.1; NZ_WUCM01000033.1.
DR RefSeq; YP_002348703.1; NC_003143.1.
DR AlphaFoldDB; Q8ZAH6; -.
DR STRING; 214092.YPO3825; -.
DR PaxDb; Q8ZAH6; -.
DR DNASU; 1145352; -.
DR EnsemblBacteria; AAM83994; AAM83994; y0405.
DR EnsemblBacteria; AAS63391; AAS63391; YP_3223.
DR GeneID; 57974883; -.
DR KEGG; ype:YPO3825; -.
DR KEGG; ypk:y0405; -.
DR KEGG; ypm:YP_3223; -.
DR PATRIC; fig|214092.21.peg.4346; -.
DR eggNOG; COG3075; Bacteria.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OMA; CFGLENQ; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..424
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT B"
FT /id="PRO_0000204571"
SQ SEQUENCE 424 AA; 45506 MW; CEC65C3081A809E7 CRC64;
MKFDVIIIGG GLAGLACGIR LAEQGKYCAI VSSGQNALHF SSGSLDLLAK LPDGQAVSQP
LSALSALAEL APEHPYSKMR NITQLDELVQ EAEALLRRCG LDIVGSSAEN HLRLTPLGSC
RPTWLSLADI PVAPLNGPLP WQRVAVIGIE GFLDFQPQMV ASALQDQGID ATADYLHLPA
LDRLRDNPSE FRAVNIARIL DLPENRQPLA DELSRLSSTA EMILLPACIG LDKSAPLDAL
RAVVGKPIQL LPTLPPSLLG MRLHQALRHR FQQLGGLVMP GDAVLRAELV DNRITGLYSR
NHGDIPLRAA QMVLASGSFF SNGLVATFDK IYEPILDLDI LSLPHRADWS HSNLFAPQPY
LQFGVNTDNH LRPLRGGVAL ENLHAIGAVL GGYDPLQQGC GAGVSLTSAV FVAEQIISEM
AVTL
