ID A0A1H9A8P2_9ACTN Unreviewed; 475 AA.
AC A0A1H9A8P2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=SAMN05421756_101510 {ECO:0000313|EMBL:SEP72857.1};
OS Microlunatus flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1036181 {ECO:0000313|EMBL:SEP72857.1, ECO:0000313|Proteomes:UP000198504};
RN [1] {ECO:0000313|Proteomes:UP000198504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6856 {ECO:0000313|Proteomes:UP000198504};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOFA01000001; SEP72857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9A8P2; -.
DR STRING; 1036181.SAMN05421756_101510; -.
DR Proteomes; UP000198504; 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 42..72
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 94..117
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 50726 MW; DC3D6854CBBF10D1 CRC64;
MTQTPGLDDL PRGTTAGGDG SGAVTAGMHV AEPTASIFDS LRAPSGDLID DCVHCGFCLP
TCPTYLLEGN ETNSPRGRIY LMKMGSAGEV GMDEEFVGNF DACLGCMACV TACPSGVQYD
HLIEAVRPQI ERHWERTPAD RAFRALVFGL FPYPSRLRPA AFFGTLYQKL GVRRLLAASG
LIGRLPARLR AMEALLPQIP LRSVVARQPS FTPAVGTTRH RVGLLSGCVQ RVFFGDVNAA
ATRVLAAEGC DVVAPPRQQC CGALSSHAGR DEEARDRARR LIDVFTEAEV ETVVVTVAGC
GSSMKEYAEL LRDDPAYADR AAAFAAKVRD ISELLVQLGP VAVRHPIDAT VAYHDACHLR
HAQGIVAEPR TALGTIPSMT VVDIPEADIC CGSAGIYNLV QPEPAEELGR RKVAHIESTR
PDAVATSNAG CLLQIRRYLD AGVPLFHPVE LIDASLRGVD PVAAQALARG GPQRL
//
