ID Q3KE46_PSEPF Unreviewed; 410 AA.
AC Q3KE46;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=glcF {ECO:0000313|EMBL:ABA73960.1};
GN OrderedLocusNames=Pfl01_2217 {ECO:0000313|EMBL:ABA73960.1};
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73960.1, ECO:0000313|Proteomes:UP000002704};
RN [1] {ECO:0000313|EMBL:ABA73960.1, ECO:0000313|Proteomes:UP000002704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73960.1,
RC ECO:0000313|Proteomes:UP000002704};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC glycolate to glyoxylate. {ECO:0000256|PIRNR:PIRNR000139}.
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:0000256|PIRNR:PIRNR000139};
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:0000256|PIRNR:PIRNR000139};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000256|PIRNR:PIRNR000139};
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DR EMBL; CP000094; ABA73960.1; -; Genomic_DNA.
DR RefSeq; WP_011333645.1; NC_007492.2.
DR AlphaFoldDB; Q3KE46; -.
DR KEGG; pfo:Pfl01_2217; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_0_6; -.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR32479:SF17; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR PIRSF; PIRSF000139; Glc_ox_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000139};
KW Electron transport {ECO:0000256|PIRNR:PIRNR000139};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000139};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR000139};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000139}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 66..89
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 410 AA; 44361 MW; 0218DF1D4C556577 CRC64;
MQTTLSPQAR QLPRAEEAES ILRTCVHCGF CNATCPTYQL LGDELDGPRG RIYLIKQVLE
GNEVTAKTQQ HLDRCLSCRN CETTCPSGVD YHNLLDIGRA VVDAAVPRPL GQRLLREGLR
NIVPNPRLFK GLVIGGQMFR ALLPDALQDK LPRDAVMPAS RPVIRHARHV LMLEGCVQPG
LSPNTNAAAA RVLDRLGISV IPAREAGCCG AVDYHLDAQA SGLDRARHNI DAWWPAIEQG
AEAIVQTASG CGAFIKDYGH LLGADPVYAE KARRVTTLAR DLVEVLRDEP LESLGIHAVQ
RLAFHCPCTL QHAQKLGGAV ESVLTRLGFS LTSVPDAHLC CGSAGTYSLT QPTLARQLRE
QKLNALESGH PDVIVTANIG CQTHLDGAGR TPVRHWIELV DAALPSVTEA
//
