ID A0A3D8HNK2_9HELI Unreviewed; 420 AA.
AC A0A3D8HNK2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=CQA37_07810 {ECO:0000313|EMBL:RDU53023.1};
OS Helicobacter sp. MIT 99-10781.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1332285 {ECO:0000313|EMBL:RDU53023.1, ECO:0000313|Proteomes:UP000256765};
RN [1] {ECO:0000313|EMBL:RDU53023.1, ECO:0000313|Proteomes:UP000256765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 99-10781 {ECO:0000313|EMBL:RDU53023.1,
RC ECO:0000313|Proteomes:UP000256765};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-2018) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDU53023.1}.
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DR EMBL; NXLM01000022; RDU53023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8HNK2; -.
DR Proteomes; UP000256765; Unassembled WGS sequence.
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:UP000256765};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 1..64
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|Pfam:PF13183"
FT DOMAIN 174..259
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
FT DOMAIN 311..394
FT /note="Cysteine-rich"
FT /evidence="ECO:0000259|Pfam:PF02754"
SQ SEQUENCE 420 AA; 47214 MW; 17494E8C7A118D9C CRC64;
MKCGKCIPSC TIYQVNRDET TSPRGFLDLL GAYKDGKLPL DSNAKKIFES CFLCTTCVSV
CPASLPTDLA IESVRVEIAK EYGISWYKRA YFFLLRHRKW ADFVFSFLAF IAPCAFKSET
YKGEKTKLCA RSFVFGLKGR SIFPFVKKSF LQRHGGEKGA LDSQAQDSQT QSRVAIFIGC
ISNYNYPNVG ESLLKILNKL NISYFVPKSQ ECCGAPAFFT GDIQTVLFLV KKNIEYFESF
WDEIDAMLIP EATCAAMLKV DWKHALELSG ESEWVKRLEK LLPKIHMASA WLQRQTDLTK
HLQEGKQQES VTYHDPCHAR KVLGIHKEPR ALLSKNFNLI EMQDSARCCG FGGISMQSSN
YALTLKAGTP KAEDIENSKA QIVSAECGAC RMQITNTLDS IGSKVRFIHP LELLAENLKS
//
