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Database: UniProt
Entry: B6JLQ4_HELP2
LinkDB: B6JLQ4_HELP2
Original site: B6JLQ4_HELP2 
ID   B6JLQ4_HELP2            Unreviewed;       433 AA.
AC   B6JLQ4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   Name=glpC {ECO:0000313|EMBL:ACJ07832.1};
GN   OrderedLocusNames=HPP12_0679 {ECO:0000313|EMBL:ACJ07832.1};
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508 {ECO:0000313|EMBL:ACJ07832.1, ECO:0000313|Proteomes:UP000008198};
RN   [1] {ECO:0000313|Proteomes:UP000008198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12 {ECO:0000313|Proteomes:UP000008198};
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACJ07832.1, ECO:0000313|Proteomes:UP000008198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12 {ECO:0000313|EMBL:ACJ07832.1,
RC   ECO:0000313|Proteomes:UP000008198};
RX   PubMed=20478826; DOI=10.1093/nar/gkq378;
RA   Fischer W., Windhager L., Rohrer S., Zeiller M., Karnholz A., Hoffmann R.,
RA   Zimmer R., Haas R.;
RT   "Strain-specific genes of Helicobacter pylori: genome evolution driven by a
RT   novel type IV secretion system and genomic island transfer.";
RL   Nucleic Acids Res. 38:6089-6101(2010).
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; CP001217; ACJ07832.1; -; Genomic_DNA.
DR   RefSeq; WP_001004844.1; NC_011498.1.
DR   AlphaFoldDB; B6JLQ4; -.
DR   KEGG; hpp:HPP12_0679; -.
DR   HOGENOM; CLU_023081_0_1_7; -.
DR   Proteomes; UP000008198; 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;  49164 MW;  1F54181634A0EA6F CRC64;
     MNENINENIF EEVGDACVKC AKCVPGCTIY RIHKDEATSP RGFLDLMRLN AQNKLQLDTN
     LKHLLETCFL CTACVEICPF HLPIDTLIEK AREKIAQKHG IAWYKKSYFS LLKNRKKMDR
     VFSTAHFLAP CIFKQVGDSL EPRAAFKGLF KRFKKSALPP LNQKSFLQKH AEIKPLENPI
     QKVAIFIGCL SNYHYQQVGE SLLYILEKLN IQAIIPNQEC CSAPAYFTGD KDTTLFLVKK
     NIEWFESYLD EVDAIIVPEA TCASMLINDY YKVFLGEKDK DLHVKRLEKI TPKIYLASVF
     LEKHTSLKSL LEKIPKGKKE VITYHNPCHA KKTLNAHKEV RNLLNLHYEI KEMPDNCCGF
     GGITMQTEKA EFSLKVGLLR AKEIIDTKAA ILSAECGACH MQLNNALKSL DDPNTPPFSH
     PLELIAKALK SAE
//
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