ID IORB_PYRKO Reviewed; 202 AA. AC O07836; Q5JFI1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 16-JUN-2009, entry version 54. DE RecName: Full=Indolepyruvate oxidoreductase subunit iorB; DE Short=IOR; DE EC=1.2.7.8; DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit beta; GN Name=iorB; OrderedLocusNames=TK0135; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius; CC -!- SUBUNIT: Heterodimer of the iorA and iorB subunits. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20529.1; Type=Frameshift; Positions=132, 148, 167, 176, 189; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D86221; BAA20529.1; ALT_FRAME; Genomic_DNA. DR EMBL; AP006878; BAD84324.1; -; Genomic_DNA. DR RefSeq; YP_182548.1; -. DR GeneID; 3235681; -. DR GenomeReviews; AP006878_GR; TK0135. DR KEGG; tko:TK0135; -. DR NMPDR; fig|69014.3.peg.303; -. DR HOGENOM; O07836; -. DR OMA; O07836; ALRYINY. DR BioCyc; TKOD69014:TK0135-MON; -. DR BRENDA; 1.2.7.8; 192130. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase ac...; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017719; Indolepyruvate_Fd_OxRdtase_bsu. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed. DR Gene3D; G3DSA:3.40.920.10; Pyrv_Fd/Flavodoxin_OxRdtase; 1. DR Pfam; PF01558; POR; 1. DR TIGRFAMs; TIGR03334; IOR_beta; 1. PE 1: Evidence at protein level; KW Complete proteome; Oxidoreductase. FT CHAIN 1 202 Indolepyruvate oxidoreductase subunit FT iorB. FT /FTId=PRO_0000099936. FT CONFLICT 158 158 Q -> K (in Ref. 1; BAA20529). FT CONFLICT 188 188 A -> S (in Ref. 1; BAA20529). SQ SEQUENCE 202 AA; 21886 MW; 2BCB29E499855B43 CRC64; MKEYNIVITG VGGQGILTAA NLLGWAALRA GYKVRVGEVH GMSQRFGSVI AYVRFGEDVY GAMVPEGKAD VILSFEPVEA LRYINYLKKG GLVFTNARPI PPVQVSMGLA TYPTLDEMKK IVEEDFGGKF MAFDAEKLAM EAGNIVTTNV VLIGALSQTP GFPLSEEQIK EVIRISVPPK TIDVNMRAFE LGVKAAKEML GL //