IORA_THEKO
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 03-AUG-2022, entry version 135.
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; 3235682; -.
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; 20764at2157; -.
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; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
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-bd_C.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR43710; PTHR43710; 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; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR03336; IOR_alpha; 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
