GLPB_ESCF3
ID GLPB_ESCF3 Reviewed; 419 AA.
AC B7LM86;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=EFER_0924;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ88459.1; -; Genomic_DNA.
DR RefSeq; WP_001209890.1; NC_011740.1.
DR AlphaFoldDB; B7LM86; -.
DR EnsemblBacteria; CAQ88459; CAQ88459; EFER_0924.
DR KEGG; efe:EFER_0924; -.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OMA; CFGLENQ; -.
DR OrthoDB; 1152849at2; -.
DR BioCyc; EFER585054:EFER_RS04730-MON; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000000745; 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..419
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT B"
FT /id="PRO_1000133363"
SQ SEQUENCE 419 AA; 45392 MW; FA205324F0B782E9 CRC64;
MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQAVTDI
HSGLESLRQQ APAHPYSLLG PQRVLDLACQ AQTLIAESGA QLQGSVEQAH QRITPLGTLR
STWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELDLSVETAE IELPELDVLR
NNATEFRAVN IARFLDNEEN WSLLLDALIP VANTCEMILM PACFGLADDK LWYWLNEKLP
CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGMVN EIWTRNHADI
PLRPRFAVLA SGSFFSGGLV AEREGIREPI VGLDVLQTAT RGEWYKGDFF APQPWQQFGV
TTDEALRPSQ AGKTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ