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Database: UniProt
Entry: H3ZRP3_THELN
LinkDB: H3ZRP3_THELN
Original site: H3ZRP3_THELN 
ID   H3ZRP3_THELN            Unreviewed;       200 AA.
AC   H3ZRP3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorB {ECO:0000256|ARBA:ARBA00017709};
DE            EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit beta {ECO:0000256|ARBA:ARBA00033011};
GN   ORFNames=OCC_13291 {ECO:0000313|EMBL:EHR77449.1};
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR77449.1, ECO:0000313|Proteomes:UP000015502};
RN   [1] {ECO:0000313|EMBL:EHR77449.1, ECO:0000313|Proteomes:UP000015502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
RC   {ECO:0000313|Proteomes:UP000015502};
RX   PubMed=22493191; DOI=10.1128/JB.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(2012).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995}.
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         Evidence={ECO:0000256|ARBA:ARBA00033657};
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC       {ECO:0000256|ARBA:ARBA00011238}.
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DR   EMBL; CP006670; EHR77449.1; -; Genomic_DNA.
DR   RefSeq; WP_004070312.1; NC_022084.1.
DR   AlphaFoldDB; H3ZRP3; -.
DR   STRING; 523849.OCC_13291; -.
DR   PaxDb; 523849-OCC_13291; -.
DR   GeneID; 16549845; -.
DR   KEGG; tlt:OCC_13291; -.
DR   HOGENOM; CLU_087284_1_1_2; -.
DR   OrthoDB; 53326at2157; -.
DR   Proteomes; UP000015502; Chromosome.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017719; Indolepyruvate_Fd_OxRdtase_bsu.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   NCBIfam; TIGR03334; IOR_beta; 1.
DR   PANTHER; PTHR43854; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR   PANTHER; PTHR43854:SF1; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORB; 1.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..194
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
SQ   SEQUENCE   200 AA;  21679 MW;  A348A7D12C0BEBF3 CRC64;
     MNVIYCGVGG QGIVLMSNIV GEACARKGIH VVSGELHGLS QRSGSVIVHQ RIGEGLSPLI
     PYGEADVILA LEPMEALRYV YFLKPGGVVI TNTRLIHHPY ETENFVKGKI DKYITYEEIV
     ENIRKSGAKL YEIDALNLAE EAGTALAQNV VLVGALTALP DFPIDKETML EAVKASVPEK
     AVEANVKAFE LGYNAMKKLL
//
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