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Database: UniProt
Entry: A0A285SCI3_9RHOB
LinkDB: A0A285SCI3_9RHOB
Original site: A0A285SCI3_9RHOB 
ID   A0A285SCI3_9RHOB        Unreviewed;       426 AA.
AC   A0A285SCI3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=SAMN05877831_104162 {ECO:0000313|EMBL:SOC05445.1};
OS   Rhodobacter maris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=446682 {ECO:0000313|EMBL:SOC05445.1, ECO:0000313|Proteomes:UP000219111};
RN   [1] {ECO:0000313|Proteomes:UP000219111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA276 {ECO:0000313|Proteomes:UP000219111};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) 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; OBMT01000004; SOC05445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285SCI3; -.
DR   OrthoDB; 9765258at2; -.
DR   Proteomes; UP000219111; 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; 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; 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}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          14..46
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          67..96
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   426 AA;  45522 MW;  5F4C01632AFD6816 CRC64;
     MQTSFTPEQL ADPGIARANE ILRACVHCGF CTATCPSYQV LGDELDSPRG RIYLIKEMLE
     TGRPADARTA KHIDRCLGCL ACMTTCPSGV DYMHLIDHAR AHVERTYKRP AGERLLRFLL
     AKIVPYPRRF RLAMKGARLA RPLAFVMPDK RLKAMLALAP AQLPKPSKND RPQVFAPTGP
     RRYRVALQTG CAQKALDTDI NDATIRLLRR LGCEVVILKL GCCGALSHHM GREGEAHAQA
     AANIRAYAAA GPLDAILINT SGCGTTVKDY GGIFEGDPLE GQAAQVAALA KDITEFLETI
     GLPQGAPKGL RVAYHSACSL QHGQKVKTAP KALLAAAGFE VVEPADPHLC CGSAGTYNLL
     QPEIAGELKR RKIATLEATA PQIIAAGNIG CMMQIGSGIG VPVVHTVQLL DWATGGPKPH
     GLAALP
//
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