ID   IORA_PYRKO              Reviewed;         647 AA.
AC   O07835; Q5JFI0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   16-JUN-2009, entry version 63.
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   Pyrococcus kodakaraensis (Thermococcus kodakaraensis).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KOD1;
RX   MEDLINE=97324592; PubMed=9180697; DOI=10.1007/s004380050436;
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
RT   oxidoreductases.";
RL   Mol. Gen. Genet. 254:433-439(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative
CC       decarboxylation of arylpyruvates.
CC   -!- CATALYTIC ACTIVITY: (Indol-3-yl)pyruvate + CoA + 2 oxidized
CC       ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO(2) + 2 reduced
CC       ferredoxin + H(+).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius;
CC   -!- SUBUNIT: Heterodimer of the iorA and iorB subunits.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; D86221; BAA20528.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD84325.1; -; Genomic_DNA.
DR   RefSeq; YP_182549.1; -.
DR   HSSP; O28604; 1JNR.
DR   GeneID; 3235682; -.
DR   GenomeReviews; AP006878_GR; TK0136.
DR   KEGG; tko:TK0136; -.
DR   NMPDR; fig|69014.3.peg.304; -.
DR   HOGENOM; O07835; -.
DR   OMA; O07835; VADDPSM.
DR   BioCyc; TKOD69014:TK0136-MON; -.
DR   BRENDA; 1.2.7.8; 192130.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase ac...; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR017721; Indolepyruvate_Fd_OxRdtase_asu.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011766; TPP_enzyme_bd_C.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Repeat; Transport.
FT   CHAIN         1    647       Indolepyruvate oxidoreductase subunit
FT                                iorA.
FT                                /FTId=PRO_0000099930.
FT   DOMAIN      585    614       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      616    645       4Fe-4S ferredoxin-type 2.
FT   METAL       625    625       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       628    628       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       631    631       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       635    635       Iron-sulfur (4Fe-4S) (Potential).
FT   CONFLICT     26     26       A -> E (in Ref. 1; BAA20528).
FT   CONFLICT     50     54       DTMAA -> IRWQT (in Ref. 1; BAA20528).
FT   CONFLICT    311    311       P -> R (in Ref. 1; BAA20528).
FT   CONFLICT    602    603       NA -> KT (in Ref. 1; BAA20528).
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
//