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Database: UniProt
Entry: IORA_THEKO
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ID   IORA_THEKO              Reviewed;         647 AA.
AC   O07835; Q5JFI0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   13-SEP-2023, entry version 139.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA;
DE            Short=IOR;
DE            EC=1.2.7.8;
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha;
GN   Name=iorA; OrderedLocusNames=TK0136;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PRESENCE OF A 3FE-4S AND TWO 4FE-4S
RP   CLUSTERS.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=9180697; DOI=10.1007/pl00008607;
RA   Siddiqui M.A., Fujiwara S., Imanaka T.;
RT   "Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1
RT   possesses a mosaic structure showing features of various oxidoreductases.";
RL   Mol. Gen. Genet. 254:433-439(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC         (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:12645, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57271,
CC         ChEBI:CHEBI:57287; EC=1.2.7.8;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000303|PubMed:9180697};
CC       Note=Binds 2 [4Fe-4S] clusters. In this family the first cluster has a
CC       non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
CC       {ECO:0000303|PubMed:9180697};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.;
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
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DR   EMBL; D86221; BAA20528.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84325.1; -; Genomic_DNA.
DR   RefSeq; WP_011249091.1; NC_006624.1.
DR   AlphaFoldDB; O07835; -.
DR   STRING; 69014.TK0136; -.
DR   EnsemblBacteria; BAD84325; BAD84325; TK0136.
DR   GeneID; 78446641; -.
DR   KEGG; tko:TK0136; -.
DR   PATRIC; fig|69014.16.peg.136; -.
DR   eggNOG; arCOG01609; Archaea.
DR   HOGENOM; CLU_017727_0_0_2; -.
DR   InParanoid; O07835; -.
DR   OMA; IGDSTFM; -.
DR   OrthoDB; 15347at2157; -.
DR   PhylomeDB; O07835; -.
DR   BRENDA; 1.2.7.8; 5246.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR   CDD; cd02008; TPP_IOR_alpha; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR045025; HACL1-like.
DR   InterPro; IPR017721; IorA.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03336; IOR_alpha; 1.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF7; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat; Transport.
FT   CHAIN           1..647
FT                   /note="Indolepyruvate oxidoreductase subunit IorA"
FT                   /id="PRO_0000099930"
FT   DOMAIN          585..614
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          616..645
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         594
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         597
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         600
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         606
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         625
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         628
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         631
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   BINDING         635
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000303|PubMed:9180697"
FT   CONFLICT        26
FT                   /note="A -> E (in Ref. 1; BAA20528)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..54
FT                   /note="DTMAA -> IRWQT (in Ref. 1; BAA20528)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="P -> R (in Ref. 1; BAA20528)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602..603
FT                   /note="NA -> KT (in Ref. 1; BAA20528)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   647 AA;  70900 MW;  AE24D283C96CDBF7 CRC64;
     MAKVTDIVLW DKPGERVLLL GNHAIARGAL EANIAVFAAY PGTPSSELTD TMAAVAKKAG
     VYMEYSTNEK VAFETALAAA WSGLRAMTAM KHVGLNVAAD SFLSSVGMGV EGGFVIMVAD
     DPSMWSSQNE QDTRVYAKFA NVPVLEPSSP HEAKEMTKYA FELSEKFKHF VILRTTTRSS
     HARGDVVLGE LPEEIKTGKR KFGKFKKDPT RFVDVPAHAR KFHPLILEKI EKIREELNNC
     PFNWIEGKED AKVGIIAPGL SYAYVKEALA WLGVEDVKIL KLGTPFPVPY GLLGKFFDGL
     EKVLIVEELE PVVEEQVKTW AYDKGLRIPI HGKDLVPRVY EMTTRRAVEA IAKFLGLETP
     INFAEIDEKY EKVSQIVPPR PPSLCPACPH RNSFFAIRKA AGPKAIYPSD IGCYTLGVLP
     PLRTVDTTVA MGASIGIGHG LSIAMNGSLA EEEHKEGKEK QIIVATIGDS TFYHTGLPAL
     ANAIYNRSNV LIVVLDNLVT AMTGDQPNPG TGQTPHGMGK RIPIEDVAKA MGADFVAVVD
     PYDIKATYET IKKALEVEGV SVVVSRQVCA LYKIGQMRRR GMKWPIYHVV EDKCTGCKIC
     INAYGCPAIY WDPETKKAKV DPTMCWGCGG CAQVCPFDAF EPMKEGE
//
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