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Database: UniProt
Entry: A0A0A0F0Z9_9GAMM
LinkDB: A0A0A0F0Z9_9GAMM
Original site: A0A0A0F0Z9_9GAMM 
ID   A0A0A0F0Z9_9GAMM        Unreviewed;       401 AA.
AC   A0A0A0F0Z9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=N800_00260 {ECO:0000313|EMBL:KGM55102.1};
OS   Lysobacter daejeonensis GH1-9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM55102.1, ECO:0000313|Proteomes:UP000029998};
RN   [1] {ECO:0000313|EMBL:KGM55102.1, ECO:0000313|Proteomes:UP000029998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GH1-9 {ECO:0000313|EMBL:KGM55102.1,
RC   ECO:0000313|Proteomes:UP000029998};
RA   Zhang S., Wang G.;
RT   "Genome sequencing of Lysobacter.";
RL   Submitted (AUG-2013) 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:KGM55102.1}.
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DR   EMBL; AVPU01000007; KGM55102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0F0Z9; -.
DR   STRING; 1385517.N800_00260; -.
DR   eggNOG; COG0247; Bacteria.
DR   Proteomes; UP000029998; 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   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:SF19; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT C; 1.
DR   PANTHER; PTHR32479; 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; 2.
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:UP000029998};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          1..26
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          45..70
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          127..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  42168 MW;  C1B47D821F033DFC CRC64;
     MADRCVQCGL CLPACPTYAR DHLEAESPRG RIAIARGLAL GSIAPSVAGD AHLDHCLACR
     SCEAVCPAGV EYGALISLQR SRQRARRPLR ALQRITEALA AHPRQLTALL RLYRWTFPLL
     PVAMRRLPRP PAAPRGRPPK PLPATTTTPA PRGNVPAVGT HPPSTSTFLA DAPSVALFAG
     CAGRGFEAPL RAQFGALCHA LGYRVVDAPG QTCCGTLHRH AGDADTATRL AADNARALSG
     IDHVLTLASG CHEAVAASVG TDGRAEDALA FLARHLDRLE WAPCPDRVAV HLPCSQRNVV
     RSTPALRRLL DAVPGLQALE LTAGTGCCGA AGTAMLEDPA RAAGYRQPLL DQLASCGATR
     LLSANLGCRL HLAGGTTIPV EHPLEFLLRL ARIKNPPPAS P
//
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