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
//