GLCE_ECOLI
ID GLCE_ECOLI Reviewed; 350 AA.
AC P52073; P76654; Q2M9L7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycolate oxidase subunit GlcE {ECO:0000305|PubMed:8606183};
DE EC=1.1.99.14 {ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183};
DE AltName: Full=Glycolate dehydrogenase subunit GlcE;
GN Name=glcE {ECO:0000303|PubMed:8606183}; Synonyms=gox, yghL;
GN OrderedLocusNames=b4468, JW5487;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8606183; DOI=10.1128/jb.178.7.2051-2059.1996;
RA Pellicer M.T., Badia J., Aguilar J.T., Baldoma L.;
RT "glc locus of Escherichia coli: characterization of genes encoding the
RT subunits of glycolate oxidase and the glc regulator protein.";
RL J. Bacteriol. 178:2051-2059(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=4557653; DOI=10.1016/0005-2728(72)90111-9;
RA Lord J.M.;
RT "Glycolate oxidoreductase in Escherichia coli.";
RL Biochim. Biophys. Acta 267:227-237(1972).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 11775;
RX PubMed=2689218; DOI=10.1016/0014-5793(89)81673-4;
RA Sallal A.K., Nimer N.A.;
RT "The intracellular localization of glycolate oxidoreductase in Escherichia
RT coli.";
RL FEBS Lett. 258:277-280(1989).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=9880556; DOI=10.1074/jbc.274.3.1745;
RA Pellicer M.T., Fernandez C., Badia J., Aguilar J., Lin E.C., Baldom L.;
RT "Cross-induction of glc and ace operons of Escherichia coli attributable to
RT pathway intersection. Characterization of the glc promoter.";
RL J. Biol. Chem. 274:1745-1752(1999).
CC -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC glycolate to glyoxylate (PubMed:4557653, PubMed:8606183). Is required
CC for E.coli to grow on glycolate as a sole source of carbon
CC (PubMed:8606183). Is also able to oxidize D-lactate ((R)-lactate) with
CC a similar rate (PubMed:4557653). Does not link directly to O(2), and
CC 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act
CC as artificial electron acceptors in vitro, but the physiological
CC molecule that functions as primary electron acceptor during glycolate
CC oxidation is unknown (PubMed:4557653). {ECO:0000269|PubMed:4557653,
CC ECO:0000269|PubMed:8606183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655; EC=1.1.99.14;
CC Evidence={ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21265;
CC Evidence={ECO:0000269|PubMed:8606183, ECO:0000305|PubMed:4557653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:4557653};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: In vitro the glycolate oxidase activity is
CC inhibited by the sulfhydryl inhibitors CuSO4 and PCMB, by KCN, but not
CC by the metal complexing agent EDTA. {ECO:0000269|PubMed:4557653}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for glycolate {ECO:0000269|PubMed:4557653};
CC KM=0.7 mM for D-lactate {ECO:0000269|PubMed:4557653};
CC Note=Parameters measured from a partially purified enzyme from
CC extracts of glycolate grown cells. {ECO:0000305|PubMed:4557653};
CC pH dependence:
CC Optimum pH is 8.0-8.8. {ECO:0000269|PubMed:4557653};
CC -!- SUBUNIT: The glycolate oxidase likely consists of three subunits, GlcD,
CC GlcE and GlcF. {ECO:0000269|PubMed:8606183}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2689218}.
CC Note=Glycolate oxidoreductase activity was shown to be firmly
CC associated with the cytoplasmic membranes.
CC {ECO:0000269|PubMed:2689218}.
CC -!- INDUCTION: Part of the glcDEFGB operon, which is induced by growth on
CC glycolate, under the positive control of GlcC. Also induced by growth
CC on acetate. Expression of the glc operon is strongly dependent on the
CC integration host factor (IHF) and is repressed by the global
CC respiratory regulator ArcA-P. {ECO:0000269|PubMed:9880556}.
CC -!- DISRUPTION PHENOTYPE: Abolishes glycolate oxidase activity. Is unable
CC to grow on glycolate as the sole source of carbon, in contrast to wild
CC type. {ECO:0000269|PubMed:8606183}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69145.1; Type=Frameshift; Note=Fuses together glcE and glcF.; Evidence={ECO:0000305};
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DR EMBL; L43490; AAB02531.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69145.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48158.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77039.1; -; Genomic_DNA.
DR RefSeq; WP_000943100.1; NZ_LN832404.1.
DR RefSeq; YP_026191.1; NC_000913.3.
DR AlphaFoldDB; P52073; -.
DR SMR; P52073; -.
DR BioGRID; 4262367; 16.
DR STRING; 511145.b4468; -.
DR jPOST; P52073; -.
DR PaxDb; P52073; -.
DR PRIDE; P52073; -.
DR DNASU; 2847718; -.
DR EnsemblBacteria; AAT48158; AAT48158; b4468.
DR EnsemblBacteria; BAE77039; BAE77039; BAE77039.
DR GeneID; 2847718; -.
DR KEGG; ecj:JW5487; -.
DR KEGG; eco:b4468; -.
DR PATRIC; fig|1411691.4.peg.3752; -.
DR EchoBASE; EB2819; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_0_0_6; -.
DR InParanoid; P52073; -.
DR OMA; PLNASCW; -.
DR PhylomeDB; P52073; -.
DR BioCyc; EcoCyc:G7544-MON; -.
DR BioCyc; MetaCyc:G7544-MON; -.
DR PRO; PR:P52073; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IBA:GO_Central.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IMP:EcoCyc.
DR GO; GO:0046296; P:glycolate catabolic process; IMP:EcoCyc.
DR GO; GO:1903457; P:lactate catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..350
FT /note="Glycolate oxidase subunit GlcE"
FT /id="PRO_0000087503"
FT DOMAIN 1..173
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 350 AA; 38361 MW; D6471A76FD354D5A CRC64;
MLRECDYSQA LLEQVNQAIS DKTPLVIQGS NSKAFLGRPV TGQTLDVRCH RGIVNYDPTE
LVITARVGTP LVTIEAALES AGQMLPCEPP HYGEEATWGG MVACGLAGPR RPWSGSVRDF
VLGTRIITGA GKHLRFGGEV MKNVAGYDLS RLMVGSYGCL GVLTEISMKV LPRPRASLSL
RREISLQEAM SEIAEWQLQP LPISGLCYFD NALWIRLEGG EGSVKAAREL LGGEEVAGQF
WQQLREQQLP FFSLPGTLWR ISLPSDAPMM DLPGEQLIDW GGALRWLKST AEDNQIHRIA
RNAGGHATRF SAGDGGFAPL SAPLFRYHQQ LKQQLDPCGV FNPGRMYAEL
