ID A0A1J0ABU4_9CYAN Unreviewed; 449 AA.
AC A0A1J0ABU4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:APB33383.1};
GN ORFNames=GlitD10_1063 {ECO:0000313|EMBL:APB33383.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB33383.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB33383.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB33383.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
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; CP017675; APB33383.1; -; Genomic_DNA.
DR RefSeq; WP_071453974.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0ABU4; -.
DR STRING; 1188229.GlitD10_1063; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000180235; 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; 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:UP000180235};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 14..42
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 62..91
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 449 AA; 50012 MW; 11ABA576870E85D8 CRC64;
MATASGFDSQ HPPSQAVIDT CVHCGFCLTT CPSYRVLGTE MDSPRGRIYQ MNAINQGEIG
LGMATVSHFD SCLGCLACVT ACPSGVRYDE LIGATRAQIQ RNVSRSGWEM LVRGVIFQLF
PYPERLRWVA PFLWLYQKMG WQRWLPGLLG RISPPLGAMA GALPPLKFSQ LLPQPWPEVL
PAQGTRRYRV GVILGCVQRL FNPQVNEATV RVLRAVGCEV VIPPQQGCCA ALPQHQGETA
QAQTLARWMI DSFRHYQLDA ILINASGCGH TLKEYGHILA DDPEYRERAQ AFSRQVKDVQ
EFLAQIDLGV PLYPLADKPL SVVYQDACHM IHGQKISLQP RQLLRQIPGV ELREPWDAAL
CCGSAGVYSF LQPETAQDLG RQKVMNLLNT GAQVIASANI GCTVQIQQYL RERTARVPVY
HPVQLLDQAM RRLPLQNVRH PRQADLVRA
//
