ID I4ICN4_9CHRO Unreviewed; 451 AA.
AC I4ICN4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=MICAI_2300009 {ECO:0000313|EMBL:CCI32058.1};
OS Microcystis sp. T1-4.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160279 {ECO:0000313|EMBL:CCI32058.1, ECO:0000313|Proteomes:UP000004501};
RN [1] {ECO:0000313|EMBL:CCI32058.1, ECO:0000313|Proteomes:UP000004501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-4 {ECO:0000313|EMBL:CCI32058.1,
RC ECO:0000313|Proteomes:UP000004501};
RA Genoscope - CEA;
RL Submitted (APR-2012) 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:CCI32058.1}.
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DR EMBL; CAIP01000147; CCI32058.1; -; Genomic_DNA.
DR RefSeq; WP_008200636.1; NZ_CAIP01000147.1.
DR AlphaFoldDB; I4ICN4; -.
DR Proteomes; UP000004501; 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 25..56
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 77..100
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 451 AA; 50092 MW; 4DE148EE100F1E73 CRC64;
MQTSEHSLNF QELIDQKSQG FDPKNPPAQE LIDSCVHCGF CLSTCPSYRV IGKEMDSPRG
RIYLMNAINK GEAVLDETTS QHFDTCLGCL ACVSTCPSGV QYDQLIAAVR PQVERNQPRS
FKDKIIRFLI FNLFPYPVRL KLFLPFLWLY QTLGLQTLVR KSGILKMLFP RLAAMESILP
QITLNSLFKN YADVIPSQTE KRYRVGVVLG CVQRLFFSPV NEATVRVLTA NGCEVVIPKI
QGCCAALPAH QGQEKQAQSL ARQMIDSFAA TEVDYIIINA AGCGHTLKEY HHILADDPEY
KDKAKEFVAK VRDAQEFLDA VGLTADLSPI TETELTLVYQ DACHLLHGQK ISVQPRQLLQ
KIPNINLKEP IDAALCCGSA GVYNMLQPDT ADQLGQQKVR NLLNTGAAVI ASPNPGCSLQ
IKKHLQLQGK DTPVIHPIEL LDYAIRGLKI S
//
