ID A0A2T1FDU1_9CYAN Unreviewed; 469 AA.
AC A0A2T1FDU1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=C7B67_24215 {ECO:0000313|EMBL:PSB43173.1};
OS filamentous cyanobacterium Phorm 6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107706 {ECO:0000313|EMBL:PSB43173.1, ECO:0000313|Proteomes:UP000239157};
RN [1] {ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|Proteomes:UP000239157};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB43173.1, ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|EMBL:PSB43173.1,
RC ECO:0000313|Proteomes:UP000239157};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) 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:PSB43173.1}.
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DR EMBL; PVWI01000269; PSB43173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1FDU1; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000239157; 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:UP000239157};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 41..72
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 93..116
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 469 AA; 51764 MW; 1D393D1B8A03CB6E CRC64;
MQTSEISQIP SEDLKPAKES NFLAQNPHLQ TLEIPGFDSN NPPDPKLIDT CVHCGFCLST
CPSYRVLGKE MDSPRGRIYL MDAINEGDAP LNEATSQHFD TCLGCLACVT TCPSGVQYDK
LISATRHQVT RNQKRTFSDN VIRTLIFNLF PYPHRLRPLL VPLFIYQKLG LPKLVRKTGL
LKKVFPRLAA MESILPEVTV DSFRDNLPEV IPAQGEKRYR VGVILGCVQR LLFSPVNEAT
VRVLTANGCE VVIPKSQGCC AALPEHQGQA EQAKALARQM IDSFENTDVD VVIINAAGCG
HTLKEYGHIL ADDPEYREKA ENFAANVKDI QEFLASAGIT AKLNPLVEGD LTIVYQDACH
LLHGQKISLQ PRQLLQQIPG VKLKEPLDAA LCCGSAGVYN MLQPEIADEL GVQKVENLLN
TGAELIASSN PGCSLQIKKH LELQGKEVTL MHPIELLDYS IRGVKLQRR
//
