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Database: UniProt
Entry: A0A0A7KJ20_9DEIO
LinkDB: A0A0A7KJ20_9DEIO
Original site: A0A0A7KJ20_9DEIO 
ID   A0A0A7KJ20_9DEIO        Unreviewed;       425 AA.
AC   A0A0A7KJ20;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=QR90_04675 {ECO:0000313|EMBL:AIZ44538.1};
OS   Deinococcus radiopugnans.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ44538.1, ECO:0000313|Proteomes:UP000030634};
RN   [1] {ECO:0000313|Proteomes:UP000030634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA   Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT   "Hymenobacter sp. DG25B genome submission.";
RL   Submitted (NOV-2014) 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};
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DR   EMBL; CP010028; AIZ44538.1; -; Genomic_DNA.
DR   RefSeq; WP_039682609.1; NZ_CP010028.1.
DR   AlphaFoldDB; A0A0A7KJ20; -.
DR   STRING; 1182571.QR90_04675; -.
DR   KEGG; dsw:QR90_04675; -.
DR   HOGENOM; CLU_023081_0_1_0; -.
DR   Proteomes; UP000030634; 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; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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:UP000030634};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          14..44
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          65..94
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   425 AA;  45251 MW;  9F2FA8DF3702C56D CRC64;
     MNNEIPVQAL GPQGEVMAHA VDACVHCGFC LPACPTYALL GDEMDSPRGR IVLMKEVLEG
     GLDLLDAAPH LDRCLGCQAC VTACPSGVPY GELITSFRGW SEPQRQRSPL DRAKRYAILK
     TLPAPKLFSV AARVGQYAKP LAPALPAALR GPLDLLPERV PAMQPSPQVT PARGQRRGRV
     AFLTGCAQQA LAPNFNAATL RVLARNGIEV VVPQGQGCCG AAALHTGARD EALRLVRANL
     DAFNPDDYDA ILSNAAGCGA GLKEYPVILH GLHDEKKAKA FAAKVQDISE YLATLAREEG
     LEPFLPTSRP LKIAYHDACH LAHAQGVRAA PRELLRMIPG VSIVEIPEGD LCCGSAGTYN
     LEQPELAGQL GARKAGHILS ITPDLIASGN IGCHTQIQSH VRRQGSAVLV MHTVEVLDLA
     YRGEL
//
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