ID   IORA_ARCFU              Reviewed;         623 AA.
AC   O28783;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA;
DE            Short=IOR;
DE            EC=1.2.7.8;
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha;
GN   Name=iorA; OrderedLocusNames=AF_1489;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:O07835};
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:0000250|UniProtKB:O07835};
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
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DR   EMBL; AE000782; AAB89760.1; -; Genomic_DNA.
DR   PIR; H69435; H69435.
DR   RefSeq; WP_010878986.1; NC_000917.1.
DR   AlphaFoldDB; O28783; -.
DR   STRING; 224325.AF_1489; -.
DR   EnsemblBacteria; AAB89760; AAB89760; AF_1489.
DR   GeneID; 24795236; -.
DR   KEGG; afu:AF_1489; -.
DR   eggNOG; arCOG01609; Archaea.
DR   HOGENOM; CLU_017727_0_0_2; -.
DR   OMA; IGDSTFM; -.
DR   OrthoDB; 20764at2157; -.
DR   PhylomeDB; O28783; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
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-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR43710; PTHR43710; 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; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR03336; IOR_alpha; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..623
FT                   /note="Indolepyruvate oxidoreductase subunit IorA"
FT                   /id="PRO_0000099925"
FT   DOMAIN          593..622
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         573
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         576
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         579
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         585
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         602
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         605
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         608
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
FT   BINDING         612
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O07835"
SQ   SEQUENCE   623 AA;  67798 MW;  9B55E1CDC3860D56 CRC64;
     MLNDVVRDAE GEKVFLLGNE AIARGAIEAG IDVFAAYPGT PSSEIADTLS DACRLLRGKM
     DFYMEYSANE KVAFEVAVGA SLAGKRAMAT MKHVGVNVAA DPLFSFAYVG ARGGFVLVTA
     DDPSMHSSQN EQDNRWYGKA AKLPVVEPSS VQEAKDYAKL CFDLSEKFGL PMILRSYTRL
     SHASGVVELG KIPEKEFSRV EWERHPETDV VLPAHARKLK PILLEKLEKI ERYFNSSEMN
     WVDEGDGDVG IIACGLSYAY TKEALENLNL NLPVLKLSSM HPLPERLIEN FVSQMKKVIV
     VEEVDPFVEL HVRAMGLAEV YGKMNGYMPM NYEYNVGRVE TGIAKALGIK PSRDYEGIVA
     ESQKLAAKAP PRPPVLCPGC PHSASFYAIR RVVDELGDAA LPSDIGCYTL GINKPLEGVD
     ITICMGASVG VSNGLAHVLN NKIIATIGDS TFIHAGIPPL INAVYNHADF VLVILDNSTT
     GMTGHQPHPG TGFRGCGEAG KAVRIEDIVR GCGVEFVEVV NPYNVRKMVD VLRRALNHDG
     VAVVIARQPC AILWSRARRR EGKIVTYKVT EDCTLCMECV NTFACPALIF DGEKVSIDQS
     LCVGCAVCAK ICPNRAIKPA KSN