ID   IORB_PYRAB              Reviewed;         202 AA.
AC   Q9UZ56; G8ZHA1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=PYRAB12980; ORFNames=PAB0857;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000250}.
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   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
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DR   EMBL; AJ248287; CAB50203.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70738.1; -; Genomic_DNA.
DR   PIR; F75038; F75038.
DR   RefSeq; WP_010868412.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZ56; -.
DR   SMR; Q9UZ56; -.
DR   STRING; 272844.PAB0857; -.
DR   EnsemblBacteria; CAB50203; CAB50203; PAB0857.
DR   GeneID; 1496684; -.
DR   KEGG; pab:PAB0857; -.
DR   PATRIC; fig|272844.11.peg.1381; -.
DR   eggNOG; arCOG01602; Archaea.
DR   HOGENOM; CLU_087284_1_1_2; -.
DR   OMA; HGMSQRF; -.
DR   OrthoDB; 120779at2157; -.
DR   PhylomeDB; Q9UZ56; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..202
FT                   /note="Indolepyruvate oxidoreductase subunit IorB"
FT                   /id="PRO_0000099934"
SQ   SEQUENCE   202 AA;  21827 MW;  EA793D738A4B1B23 CRC64;
     MKEYNIVITG VGGQGILTAA NLLGWAALRA GYKVRVGEVH GMSQRFGSVI AYVRFGEDVY
     GAMVPEGKAD VILSFEPVEA LRYINYLKKG GLVFTNARPI PPVQVSMGLA SYPSMEEIRK
     IVEEDFGGKF LAFDAEKLAI EAGNVITTNV VLIGALTQTP GFPLSAEHVK EVIRISVPPK
     AVDVNMRAFE LGVKAAKEML NL