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Database: UniProt
Entry: A0A0C2R6D0_9BACL
LinkDB: A0A0C2R6D0_9BACL
Original site: A0A0C2R6D0_9BACL 
ID   A0A0C2R6D0_9BACL        Unreviewed;       378 AA.
AC   A0A0C2R6D0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=KP78_21640 {ECO:0000313|EMBL:KIL45815.1};
OS   Jeotgalibacillus soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL45815.1, ECO:0000313|Proteomes:UP000031938};
RN   [1] {ECO:0000313|EMBL:KIL45815.1, ECO:0000313|Proteomes:UP000031938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P9 {ECO:0000313|EMBL:KIL45815.1,
RC   ECO:0000313|Proteomes:UP000031938};
RA   Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT   "Genome sequencing of Jeotgalibacillus soli.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIL45815.1}.
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DR   EMBL; JXRP01000017; KIL45815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2R6D0; -.
DR   STRING; 889306.KP78_21640; -.
DR   PATRIC; fig|889306.3.peg.2178; -.
DR   Proteomes; UP000031938; Unassembled WGS sequence.
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   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   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; PF00037; Fer4; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031938};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          10..35
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   378 AA;  42124 MW;  37B0D17A93D0D715 CRC64;
     MKLAAEGKIS LDEISDSLDL CLGCRACETA CPTNVQYGKI LESFKVAKSE SNQSPFIEKL
     ALQNALPNKF WQKAAVRTLG IYQKTKLNKL ARKSGLLRVL PERLRAFEEI TPVVQPPKRK
     VRQNTILPKK AKLNVAFFTG CVMDVFFAKI NDLSIRLLEH AGCHVTIIKE QTCCGALQHH
     SGDKSFTKKL AKENITAFEQ AEYDYVVNSI GGCGAMLVEY DKLLENEPQW VERAEKFAKK
     NIDISVILSS LGISFEKEIN KVVTYQPSCH LLNVQKVKDD PVKLITSIPG LTYLPLPQAD
     MCCGSAGIYN IVHYEESMDI LDEKMKHVHT VRPAVIVTSN PGCHLQMCLG VKREGLEKKI
     RVVHIVELLA EACGIEAV
//
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