ID C1DTK6_SULAA Unreviewed; 418 AA.
AC C1DTK6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN OrderedLocusNames=SULAZ_0451 {ECO:0000313|EMBL:ACN99075.1};
OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium.
OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN99075.1, ECO:0000313|Proteomes:UP000001369};
RN [1] {ECO:0000313|EMBL:ACN99075.1, ECO:0000313|Proteomes:UP000001369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825
RC {ECO:0000313|Proteomes:UP000001369};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001229; ACN99075.1; -; Genomic_DNA.
DR RefSeq; WP_012674394.1; NC_012438.1.
DR AlphaFoldDB; C1DTK6; -.
DR STRING; 204536.SULAZ_0451; -.
DR KEGG; saf:SULAZ_0451; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_0; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000001369; 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:SF20; 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; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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:UP000001369};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 7..37
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 418 AA; 47391 MW; 98F9DDDCB1ED3704 CRC64;
MSHYIEPKLT IELAHQCVKC SACRQVCPTY SVVKEERSSP RGRLALAEAV VDGILPLTED
IAAQWNQCAM CRRCEWICPN EVEYKEIMFR ARNMAKEKSK KDYFKNVVFK GLAMMGNPLT
KIGMKFAPAL MEAYGKMLGK EVPEYNAVYI DVGIPKYAKL MPKPSAKPFG LRGKEVKSEK
SKGRLLFFTG CMIDAFQGKV GESVLKLMEK AGYDVVVPKD IRCCGAPHLY SGEIDSFNKL
MKHNKQEIDK YQFDYIVVAC PTCGGALKEE YKYPVKDFAE ILEEEGFFTF RGKGEKVTFH
FPCHSYTAMK TDPNVFRNVL KNVKDANYVE GEEAMMCCGF AGYFSVANYE VASELQKRKI
EDLKKTQATY VLSDCPGCVL NLADGMYKHG DYKNVKVMHL AEYLAERLED ESVSEERK
//
