ID C5ZX11_9HELI Unreviewed; 429 AA.
AC C5ZX11;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=HCAN_0965 {ECO:0000313|EMBL:EES89679.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89679.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES89679.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(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; CM000776; EES89679.1; -; Genomic_DNA.
DR RefSeq; WP_006655667.1; NZ_DS990368.1.
DR AlphaFoldDB; C5ZX11; -.
DR STRING; 537970.HCAN_0965; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_7; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000007032; 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; 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:UP000007032};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 14..80
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT DOMAIN 181..265
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
FT DOMAIN 318..400
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
SQ SEQUENCE 429 AA; 49425 MW; B1E1BFDD1EBD7ABA CRC64;
MEHFKDYNYL KTSDACVKCG KCLPDCTIFN INGDEATSPR GFIDLLGAYQ RKEIPLDKNA
KNIFETCFLC TTCVSVCPNS LPTDTLIENI RYEIAQKYGI AWFKRIFFYL LKHRKIMDLS
MKLGAFFTPL LFQKTDDNHS IKPRFKLPFI SNRIFGAIQT KSFLNSHQEN LIYHKDNPKK
VAIFIGCLGN YNYKSVGESL VFILQKLGIN TMIPKKQKCC GAPAYFTGDF ESVNQLITEN
IAYFESFIDE VEAILIPEAT CAAMILEDWE RFMEKNPSYQ QRIQKLLPKI HMATHWLMHN
TNLKDYLSTL PKSQETFTYH DPCHARKVLG IWKEPRELLR QNYDLIEMED PNTCCGFGGV
TMQTERFNLA SKVGSKKAKM IDKTQAKYVV AECSACRMQL NNALHQEKVK TLFAHPLELI
EKAIKTARI
//
