IORB_THEKO
ID IORB_THEKO Reviewed; 202 AA.
AC O07836; Q5JFI1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
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 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].
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 -!- 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; Evidence={ECO:0000305};
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DR EMBL; D86221; BAA20529.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP006878; BAD84324.1; -; Genomic_DNA.
DR RefSeq; WP_011249090.1; NC_006624.1.
DR AlphaFoldDB; O07836; -.
DR SMR; O07836; -.
DR STRING; 69014.TK0135; -.
DR EnsemblBacteria; BAD84324; BAD84324; TK0135.
DR GeneID; 3235681; -.
DR KEGG; tko:TK0135; -.
DR PATRIC; fig|69014.16.peg.135; -.
DR eggNOG; arCOG01602; Archaea.
DR HOGENOM; CLU_087284_1_1_2; -.
DR InParanoid; O07836; -.
DR OMA; HGMSQRF; -.
DR OrthoDB; 120779at2157; -.
DR PhylomeDB; O07836; -.
DR BRENDA; 1.2.7.8; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.920.10; -; 1.
DR InterPro; IPR017719; Indolepyruvate_Fd_OxRdtase_bsu.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF53323; SSF53323; 1.
DR TIGRFAMs; TIGR03334; IOR_beta; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..202
FT /note="Indolepyruvate oxidoreductase subunit IorB"
FT /id="PRO_0000099936"
FT CONFLICT 158
FT /note="Q -> K (in Ref. 1; BAA20529)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> S (in Ref. 1; BAA20529)"
FT /evidence="ECO:0000305"
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
