IORA_PYRHO
ID IORA_PYRHO Reviewed; 648 AA.
AC O58495;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PH0765;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29856.1; -; Genomic_DNA.
DR PIR; F71124; F71124.
DR RefSeq; WP_010884856.1; NC_000961.1.
DR AlphaFoldDB; O58495; -.
DR STRING; 70601.3257173; -.
DR DNASU; 1443091; -.
DR EnsemblBacteria; BAA29856; BAA29856; BAA29856.
DR GeneID; 1443091; -.
DR KEGG; pho:PH0765; -.
DR eggNOG; arCOG01609; Archaea.
DR OMA; IGDSTFM; -.
DR OrthoDB; 20764at2157; -.
DR Proteomes; UP000000752; 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 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; PF12838; Fer4_7; 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; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Repeat; Transport.
FT CHAIN 1..648
FT /note="Indolepyruvate oxidoreductase subunit IorA"
FT /id="PRO_0000099929"
FT DOMAIN 585..614
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 616..645
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 594
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 597
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 600
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 606
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 625
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 628
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 631
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 635
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
SQ SEQUENCE 648 AA; 71532 MW; 75A843815FCE08B1 CRC64;
MVKVTDIVLW DKPGEKVLLL GNQAIVRGAL EGNIGVYAAY PGTPSSEITD TMAMVAKKAG
VYMEYSTNEK VAFETALSAS WAGLRAMTAM KHVGLNVAMD SFMTVSYMGI NGGLIVVVAD
DPSMWSSQNE QDTRAIAKFA NIPVLEPSSV QEAKDMVKYA FEISEKYGQM VILRTTTRSS
HMRGDVVLGE LPQEIKEGKR KFGNFKKNPE KYVDIPAFQR PKHPWLLETI EKFREEFNTS
PFNWIEGPED AKVGIIAPGL SYAYVKEALA WLGIDNVKIL KLGTPFPVPY GLLEKFFNGL
ERVLIVEELE PVVEEQVKVW AFDNNINIEI HGKDLVPRVY EMTTRRAVEA VAKFLGVETP
INFQEIDEKY KKVQEMVPPR PPSLCPACPH RNTFFAIRKA ATPRAIFPSD IGCYTLGVLP
PLKTVDTTIA MGGSIGVAHG LSIALNGALG EEQRKTGKEK KIIVATIGDS TFFHTGLPAL
ANAIYNRSNV LIVVMDNMVT AMTGDQPNPG TGETPHGPGK RILIEEVARA MGADFVAVVD
PYDIKETYET IKKALEVEGV SVVVSRRACA LYRIGQLRRE GKQWPIYQVN EEKCTGCKIC
INAYGCPAIY WDAEKKKARV DPLMCWGCGG CAQVCPFGAF EKVREGEL
