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Entry: A0A0F7IF54_9EURY
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ID   A0A0F7IF54_9EURY        Unreviewed;       623 AA.
AC   A0A0F7IF54;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|ARBA:ARBA00017710, ECO:0000256|PIRNR:PIRNR006439};
DE            Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE            EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812, ECO:0000256|PIRNR:PIRNR006439};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|ARBA:ARBA00030514, ECO:0000256|PIRNR:PIRNR006439};
GN   ORFNames=GAH_01011 {ECO:0000313|EMBL:AKG91665.1};
OS   Geoglobus ahangari.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Geoglobus.
OX   NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91665.1, ECO:0000313|Proteomes:UP000034723};
RN   [1] {ECO:0000313|EMBL:AKG91665.1, ECO:0000313|Proteomes:UP000034723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=234 {ECO:0000313|EMBL:AKG91665.1,
RC   ECO:0000313|Proteomes:UP000034723};
RA   Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA   Kashefi K.;
RT   "The complete genome sequence of the hyperthermophilic, obligate iron-
RT   reducing archaeon Geoglobus ahangari strain 234T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995,
CC       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|ARBA:ARBA00033657,
CC         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   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC       {ECO:0000256|ARBA:ARBA00011238, ECO:0000256|PIRNR:PIRNR006439}.
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DR   EMBL; CP011267; AKG91665.1; -; Genomic_DNA.
DR   RefSeq; WP_048095052.1; NZ_CP011267.1.
DR   AlphaFoldDB; A0A0F7IF54; -.
DR   STRING; 113653.GAH_01011; -.
DR   GeneID; 24803585; -.
DR   KEGG; gah:GAH_01011; -.
DR   PATRIC; fig|113653.22.peg.1009; -.
DR   HOGENOM; CLU_017727_0_0_2; -.
DR   InParanoid; A0A0F7IF54; -.
DR   OrthoDB; 19071at2157; -.
DR   Proteomes; UP000034723; Chromosome.
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   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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; 3.40.50.920; -; 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   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03336; IOR_alpha; 1.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF7; 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   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR006439};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   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|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR006439}; Pyruvate {ECO:0000313|EMBL:AKG91665.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034723};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          595..623
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         575
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         578
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         581
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         587
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         604
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         607
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         610
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         614
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ   SEQUENCE   623 AA;  67886 MW;  88C5C3D9A1FBAB7A CRC64;
     MLKDVILDEP GKRVFLLGNE AIARGAIEAG IDVFSAYPGT PSSEITDTLN SACKHLRGRM
     EYRMEYAVNE KVAFEVAIGA SLAGKRGMTA MKHVGLNVAA DSLFSFAYVG ARGGFVCVSA
     DDPSMHSSQN EQDNRWYGIA AKVPVVEPSS VGEAKEMVKL AFDLSERFGL PFILRSYTRL
     SHSSGIVELG EIPEKRLKKV RWERHPDTDV VLPAHARRLK PILQKKLADL EDFFTSSDIN
     WVDEADGKRG IIACGMSYNY AVEALENLGV EMPVLKLSSM NPLPRKLIAD FLANLDEVLV
     VEEVDPVVEL QVRAMAKELD VEVHGKMDGY LPENFEYNVS IVQKGIARLG GKSYDYAHLL
     ETAKSMAEIA PPRPPVLCPG CPHTATFYAI RKVVNELGNA SLPSDIGCYT LGINKPLEAV
     DITICMGASV GTSNGLSYVL DDAIIATIGD STFFHTGIPP LVNAVYNGNR FVLVVLDNST
     TGMTGHQPHP GVDARGCGEK GHAVRIEDVC RAIGVRFVEV VKSYNIRAME DALRRALKHD
     GPAVIVSKQP CAILWNRERK AKGIRITPFE VGEGCMECMK CVREFTCPAI YIQDGRPVID
     PALCAGCGVC AAVCPYRAIK PAR
//
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