ID A0A1X6YKH6_9RHOB Unreviewed; 458 AA.
AC A0A1X6YKH6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=lutA {ECO:0000313|EMBL:SLN23892.1};
GN ORFNames=ROJ8625_00974 {ECO:0000313|EMBL:SLN23892.1};
OS Roseivivax jejudonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1529041 {ECO:0000313|EMBL:SLN23892.1, ECO:0000313|Proteomes:UP000193570};
RN [1] {ECO:0000313|EMBL:SLN23892.1, ECO:0000313|Proteomes:UP000193570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8625 {ECO:0000313|EMBL:SLN23892.1,
RC ECO:0000313|Proteomes:UP000193570};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFK01000001; SLN23892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YKH6; -.
DR OrthoDB; 9765258at2; -.
DR Proteomes; UP000193570; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193570};
KW 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 458 AA; 50110 MW; 8CCD18E04F423E5D CRC64;
MQTTFTDAQL RDPDTARSNE ILRACVHCGF CTATCPTYQV LGDELDSPRG RIYLIKDMLE
NERVPDEKTV RHIDRCLSCL ACMTTCPSGV HYMHLVDHAR TYIEEHYERP WQDRALRWVL
ARILPYPGRF RVALLGAKIG RPFRALVPDR RLRAMLDMAP ATIPPVSRND DPQTFPAEGR
RRRRVALMTG CAQRALNTDI NDATIRLLTR LGCEVVVADG QGCCGALTHH MGKTDEAHGT
AARNIRAWTR EMDGDGLDAI VINTSGCGTT VKDYGHMFRT EPLAADAARV SGIAVDVSEL
LAELVREAET ETGNEAAEGI AGTDAPAGHG VFAPPRPEGH GLRVAYHAAC SLQHGQQIKS
HPKDLLKRAG FEVVEPADSH LCCGSAGTYN LMQPEISAQL KDRKVRTLEA KRPEIIAAGN
IGCMMQIGAG TEVPVVHTVE LLDWAWGGPR PPALPAPD
//
