ID A0A073CCR7_PLAAG Unreviewed; 468 AA.
AC A0A073CCR7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=glcF {ECO:0000313|EMBL:KEI65428.1};
GN ORFNames=A19Y_0185 {ECO:0000313|EMBL:KEI65428.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI65428.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI65428.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI65428.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
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; CM002803; KEI65428.1; -; Genomic_DNA.
DR RefSeq; WP_042151234.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CCR7; -.
DR STRING; 388467.A19Y_0185; -.
DR GeneID; 77286478; -.
DR PATRIC; fig|388467.6.peg.135; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_3; -.
DR Proteomes; UP000027395; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:RHEA.
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 Oxidoreductase {ECO:0000313|EMBL:KEI65428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 39..70
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 90..114
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 51578 MW; 23F4DCFCF8A11069 CRC64;
MQTSDQIIDP KSIPAKQSNF LGQNPHLNPT EIPGFDSTNP PNPNLISTCV HCGFCLSTCP
SYRVLGTEMD SPRGRIYLMD AISKNDAALG ETSAQHFDTC LGCLACVTTC PSGVKYDQLI
AATRPQIERN VPRSLSDRLI RGLIFNLFPY PKRLQAFLIP LFIYQKLGLQ KIVRQTGLLP
KISPRLAAME SILPAIPKDA FREDFPVIIP TQGEKRYRVG VILGCVQRLL FNPVNEATVR
VLTANGCEVV IPRNQGCCGA LPEHQGQTEQ SHTLIKQMID RFSGTRLDGI IINAAGCGHT
LKEYGHILKD DPQYREAAQE FSAKVKDIQE FLVEIGLTTP LSPLTETGEL TIVYQDACHL
LHGQKISSQP RQLLQQIPGV KLREPIDASL CCGSAGIYNL LQPEIAEELG QQKVDNLTNT
GAELIASSNP GCSLQIKKHL QLQGKDINLM HPMELLDYSI RGVKINIL
//
