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Entry: A0A073IVF1_9BACT
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ID   A0A073IVF1_9BACT        Unreviewed;       598 AA.
AC   A0A073IVF1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, 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=EH55_01770 {ECO:0000313|EMBL:KEJ93525.1};
OS   Synergistes jonesii.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Synergistes.
OX   NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ93525.1, ECO:0000313|Proteomes:UP000027665};
RN   [1] {ECO:0000313|EMBL:KEJ93525.1, ECO:0000313|Proteomes:UP000027665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=78-1 {ECO:0000313|EMBL:KEJ93525.1,
RC   ECO:0000313|Proteomes:UP000027665};
RA   Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT   "Draft Genome Sequence of Synergistes jonesii.";
RL   Submitted (APR-2014) 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         ECO:0000256|PIRSR:PIRSR006439-50};
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, ECO:0000256|PIRSR:PIRSR006439-50};
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:KEJ93525.1}.
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DR   EMBL; JMKI01000002; KEJ93525.1; -; Genomic_DNA.
DR   RefSeq; WP_037974011.1; NZ_JQEL01000001.1.
DR   AlphaFoldDB; A0A073IVF1; -.
DR   STRING; 2754.EH55_01770; -.
DR   PATRIC; fig|2754.20.peg.313; -.
DR   eggNOG; COG4231; Bacteria.
DR   OrthoDB; 9804603at2; -.
DR   Proteomes; UP000027665; 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; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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   NCBIfam; TIGR03336; IOR_alpha; 1.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF6; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006439};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR006439};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006439};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW   Pyruvate {ECO:0000313|EMBL:KEJ93525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027665};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..598
FT                   /note="Indolepyruvate oxidoreductase subunit IorA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001690058"
FT   DOMAIN          536..565
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          566..595
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         545
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         548
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         551
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         557
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         575
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         578
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         581
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         585
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ   SEQUENCE   598 AA;  63586 MW;  CE0544D912B1B02E CRC64;
     MSVKVCMGNE AIALGALAAG VSVAAGYPGT PSTEIIETLV GIHKPGVSVQ WSTNEKAALE
     VAAGAAYAGA RSLCTMKQVG LNVASDPLMS LSYIGVKGGM VIAVADDPGP WSSQTEQDTR
     GFAKHANLPV FDPSSPEEAY MMVLSAYEFS EKYSLPAFLR PTTRVCHASA DVDFDIDAEI
     KKSDGFEKRP EWCIFPALSY RRHGELEEKQ GEMARDFDKM PYNRIEGRGR KGVAVSGVSY
     LYAKEAIAEL GADVLLYKVG TPYPMPERLT KKFISSVDSV LVVEELDPVV EEQLLIEAAG
     RVPVLGKRSG DMPKNGEYSF EIVKKALIKY LGLPQEKEER EELPQLPVRP PVLCAGCPHR
     ASFYAAKVAT KDLKKAIYCG DIGCYTLGNA APLNMVDTCL CMGAGITIAQ GLALADAGAK
     CLAFIGDSTF FHTGIPGVIN AVYQGTDITV IVLDNRTTAM TGQQPHPGTG KRALGDDAPA
     LDIETILRAC GVKRVSRVNP FDFESAVGAI REAVGFAGVS AVIAEAPCVA QLKKPEAICF
     VNDKCIKCGR CIKEIGCPAI TPDEAGRAVV NAPLCTGCGL CACVCPVSAI ERGERNGK
//
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