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Database: UniProt
Entry: K9E0S4_9BACE
LinkDB: K9E0S4_9BACE
Original site: K9E0S4_9BACE 
ID   K9E0S4_9BACE            Unreviewed;       530 AA.
AC   K9E0S4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|PIRNR:PIRNR006439};
DE            Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE            EC=1.2.7.8 {ECO:0000256|PIRNR:PIRNR006439};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|PIRNR:PIRNR006439};
GN   ORFNames=HMPREF9447_03556 {ECO:0000313|EMBL:EKU89231.1};
OS   Bacteroides oleiciplenus YIT 12058.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=742727 {ECO:0000313|EMBL:EKU89231.1, ECO:0000313|Proteomes:UP000009872};
RN   [1] {ECO:0000313|EMBL:EKU89231.1, ECO:0000313|Proteomes:UP000009872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12058 {ECO:0000313|EMBL:EKU89231.1,
RC   ECO:0000313|Proteomes:UP000009872};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides oleiciplenus YIT 12058.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
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|PIRNR:PIRNR006439};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006439};
CC       Note=Binds 2 [4Fe-4S] clusters. In this family the first cluster has a
CC       non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
CC       {ECO:0000256|PIRNR:PIRNR006439};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKU89231.1}.
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DR   EMBL; ADLF01000015; EKU89231.1; -; Genomic_DNA.
DR   RefSeq; WP_009131086.1; NZ_JH992943.1.
DR   AlphaFoldDB; K9E0S4; -.
DR   STRING; 742727.HMPREF9447_03556; -.
DR   PATRIC; fig|742727.4.peg.3627; -.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_017727_0_0_10; -.
DR   OrthoDB; 9804603at2; -.
DR   Proteomes; UP000009872; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02008; TPP_IOR_alpha; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR045025; HACL1-like.
DR   InterPro; IPR017721; IorA.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006439};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW   Pyruvate {ECO:0000313|EMBL:EKU89231.1};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          15..181
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          380..513
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   530 AA;  57978 MW;  A90C9D79BBF3ACC9 CRC64;
     MSKQLLLGDE AIAQAALDAG LSGVYAYPGT PSTEITEYIQ TAPITAEQNI HSRWSSNEKT
     AMEAALGMSF VGKRALVCMK HVGMNVAADC FINSAVTGVK GGLIVVAADD PSMHSSQNEQ
     DSRFYGDFSL IPMYEPSNQQ EAYDMIYNGF AFSERISEPI LLRMVTRLAH SRSGVEQKTQ
     QPQNEISFSE DPRQFILLPG NARKRYRDLL ERQAEFIEAS ENSPYNKYID GPNKKMGIIA
     CGIGYNYLME NYPEGCEYPV LKIGQYPLPK KQLLQLVEAC DEILVLEDGQ PFVEKQLKGY
     LGIGVKVKGR LDGTLSQDGE LNPDKVARSV GKENKSGFGI PSLVEMRPPA LCEGCGHRDM
     YTVLTQVLKE EYPAHKVFSD IGCYTLGASA PFNAINSCVD MGASITMAKG AADGGLHPAV
     AVIGDSTFTH SGMTGLLDCV NENTNVTIII SDNETTAMTG GQDSAGTGRI EAICTGIGVA
     PEHIRVVVPL KKNYEEMKQI IREEIEYRGV SVIIPRRECI QTLARKKRNK
//
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