GLCF_ECOLI
ID GLCF_ECOLI Reviewed; 407 AA.
AC P52074; P76654; Q2M9L8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000305|PubMed:8606183};
DE EC=1.1.99.14 {ECO:0000269|PubMed:4557653, ECO:0000305|PubMed:8606183};
DE AltName: Full=Glycolate dehydrogenase subunit GlcF;
DE AltName: Full=Glycolate oxidase subunit GlcF {ECO:0000305|PubMed:8606183};
GN Name=glcF {ECO:0000303|PubMed:8606183}; Synonyms=gox, yghL;
GN OrderedLocusNames=b4467, JW5486;
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,
RP SUBCELLULAR LOCATION, AND 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000255|PROSITE-ProRule:PRU00711};
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 ECO:0000305|PubMed:8606183}. Note=Glycolate oxidoreductase activity was
CC shown to be firmly associated with the cytoplasmic membranes
CC (PubMed:2689218). And the GlcF subunit itself could only be detected in
CC the membrane fraction (PubMed:8606183). {ECO:0000269|PubMed:2689218,
CC ECO:0000269|PubMed:8606183}.
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=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L43490; AAB02532.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69145.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAT48157.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77038.1; -; Genomic_DNA.
DR RefSeq; WP_001194661.1; NZ_SSUV01000003.1.
DR RefSeq; YP_026190.1; NC_000913.3.
DR AlphaFoldDB; P52074; -.
DR SMR; P52074; -.
DR BioGRID; 4262366; 14.
DR STRING; 511145.b4467; -.
DR jPOST; P52074; -.
DR PaxDb; P52074; -.
DR PRIDE; P52074; -.
DR EnsemblBacteria; AAT48157; AAT48157; b4467.
DR EnsemblBacteria; BAE77038; BAE77038; BAE77038.
DR GeneID; 2847717; -.
DR KEGG; ecj:JW5486; -.
DR KEGG; eco:b4467; -.
DR PATRIC; fig|1411691.4.peg.3753; -.
DR EchoBASE; EB3076; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_6; -.
DR InParanoid; P52074; -.
DR OMA; VYQDACH; -.
DR PhylomeDB; P52074; -.
DR BioCyc; EcoCyc:MON0-561; -.
DR BioCyc; MetaCyc:MON0-561; -.
DR PRO; PR:P52074; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046296; P:glycolate catabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR012257; Glc_ox_4Fe-4S.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR32479:SF17; PTHR32479:SF17; 1.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR PIRSF; PIRSF000139; Glc_ox_4Fe-4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..407
FT /note="Glycolate oxidase iron-sulfur subunit"
FT /id="PRO_0000159258"
FT DOMAIN 14..47
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 66..95
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 407 AA; 45110 MW; F983C893063F76DC CRC64;
MQTQLTEEMR QNARALEADS ILRACVHCGF CTATCPTYQL LGDELDGPRG RIYLIKQVLE
GNEVTLKTQE HLDRCLTCRN CETTCPSGVR YHNLLDIGRD IVEQKVKRPL PERILREGLR
QVVPRPAVFR ALTQVGLVLR PFLPEQVRAK LPAETVKAKP RPPLRHKRRV LMLEGCAQPT
LSPNTNAATA RVLDRLGISV MPANEAGCCG AVDYHLNAQE KGLARARNNI DAWWPAIEAG
AEAILQTASG CGAFVKEYGQ MLKNDALYAD KARQVSELAV DLVELLREEP LEKLAIRGDK
KLAFHCPCTL QHAQKLNGEV EKVLLRLGFT LTDVPDSHLC CGSAGTYALT HPDLARQLRD
NKMNALESGK PEMIVTANIG CQTHLASAGR TSVRHWIEIV EQALEKE
