ID K9UTM0_9CYAN Unreviewed; 451 AA.
AC K9UTM0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=Cal6303_0094 {ECO:0000313|EMBL:AFY99202.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFY99202.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFY99202.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFY99202.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-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};
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DR EMBL; CP003610; AFY99202.1; -; Genomic_DNA.
DR RefSeq; WP_015195861.1; NC_019751.1.
DR AlphaFoldDB; K9UTM0; -.
DR STRING; 1170562.Cal6303_0094; -.
DR KEGG; calt:Cal6303_0094; -.
DR PATRIC; fig|1170562.3.peg.102; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_3; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000010477; Chromosome.
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; SSF46548; alpha-helical ferredoxin; 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:UP000010477};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 24..55
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 75..99
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 451 AA; 49916 MW; 94821EE00D4A76E7 CRC64;
MQTSENPLQE TANIKNLPGF DPINPPDPKL IDSCVHCGFC LSTCPSYRVL GKEMDSPRGR
IYLMDAINEG EIALNTATVE HFDSCLGCLA CVTTCPSGVQ YDKLISATRH QVERNYSRSW
IDNLVRKLIF SLFPYPNLLR IFLIPLFIYQ KLGIQKLIRA TGLLKLISPR LAAMDSILPE
VTLKTFQNNL PTIIPSQTEK KYRVGVILGC VQRLFFSPVN EATVRVLTAN GCEVVIPKSQ
GCCAALPEHQ GQTEQAKALA RQMIDSFADT EVDYIIINAA GCGHTLKEYH HILENDPEYA
QKAKDFVAKV RDAQEFLADV GLTSKLSPIS NKLLTMVYQD ACHLLHGQKI SVQPRQLLRQ
IPEVTIKEPL DAALCCGSAG VYNMLQPEVA EELGQQKVTN LLNTGAELIA SPNPGCALQI
NKHLQLQGKS ISVMHPMELL DLAIRGEKLK L
//
