ID B5Z739_HELPG Unreviewed; 433 AA.
AC B5Z739;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN OrderedLocusNames=HPG27_628 {ECO:0000313|EMBL:ACI27388.1};
OS Helicobacter pylori (strain G27).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI27388.1, ECO:0000313|Proteomes:UP000001735};
RN [1] {ECO:0000313|EMBL:ACI27388.1, ECO:0000313|Proteomes:UP000001735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27 {ECO:0000313|EMBL:ACI27388.1,
RC ECO:0000313|Proteomes:UP000001735};
RX PubMed=18952803; DOI=10.1128/JB.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(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; CP001173; ACI27388.1; -; Genomic_DNA.
DR RefSeq; WP_001004869.1; NC_011333.1.
DR AlphaFoldDB; B5Z739; -.
DR KEGG; hpg:HPG27_628; -.
DR HOGENOM; CLU_023081_0_1_7; -.
DR Proteomes; UP000001735; 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}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 15..81
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT DOMAIN 183..266
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
FT DOMAIN 322..403
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
SQ SEQUENCE 433 AA; 49270 MW; C7AED6ABB8445DD3 CRC64;
MNENINGNIF EEVGDACVKC AKCVPGCTIY RIHKDEATSP RGFLDLMRLN AQNKLQLDTN
LKHLLETCFL CTACVEICPF HLPIDTLIEK AREKIAQKHG IAWYKKSYFS LLKNRKKMDR
VFSTAHFLAP CIFKQVGDSL EPRAVFKGLF KRFKKSALPP LNQKSFLQKH TEVKPLENPI
QKVAIFIGCL SNYHYQQVGE SLLYILEKLN IQAIIPKQEC CSAPAYFTGD KDTTLFLVKK
NIEWFESYLD EVDAIIVPEA TCASMLINDY YKVFLGEKDK DLYVERLEKI TPKIYLASVF
LEKHTPLKNL LEKIPKGKKE SITYHNPCHA KKTLNAHKEV RNLLNSHYEI KEMPDNCCGF
GGITMQTEKA EFSLKVGLLR AKEIMDTQAR ILSAECGACH MQLNNALKSL DDPNTPSFSH
PLELIAKALK SAE
//
