IORA_PYRAB
ID IORA_PYRAB Reviewed; 648 AA.
AC Q9UZ57; G8ZHA0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, 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=PYRAB12970; ORFNames=PAB0855;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248287; CAB50202.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70737.1; -; Genomic_DNA.
DR PIR; E75038; E75038.
DR RefSeq; WP_010868411.1; NC_000868.1.
DR AlphaFoldDB; Q9UZ57; -.
DR STRING; 272844.PAB0855; -.
DR EnsemblBacteria; CAB50202; CAB50202; PAB0855.
DR GeneID; 1496683; -.
DR KEGG; pab:PAB0855; -.
DR PATRIC; fig|272844.11.peg.1380; -.
DR eggNOG; arCOG01609; Archaea.
DR HOGENOM; CLU_017727_0_0_2; -.
DR OMA; IGDSTFM; -.
DR OrthoDB; 20764at2157; -.
DR PhylomeDB; Q9UZ57; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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_0000099928"
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; 71355 MW; 069AD8E4052098F4 CRC64;
MVKVTDIVLW DKPGERVLLL GNQAIVRGAL EGNIGVYAAY PGTPSSEITD TMAAVASRAG
VYMEYSTNEK VAFETALSAS WAGLRAMTAM KHVGLNVAMD SFMTVSYMGV NGGLVVVVAD
DPSMWSSQNE QDTRAIAKFA NIPVLEPSSV QEAKDMVKYA FEISEKYGQM VILRTTTRSS
HMRGDVVLGE LPQEIKEGKR KFGDFKKNPE RYVDIPAFQR PKHKWLLETI EKFREEFNNS
PFNWIEGPED AKVGIIAPGL SYAYVKEALA WLGVDNVKVL KLGTPFPVPY GLLEKFFQGL
ERVLIVEELE PVVEEQVKVW AFDKGINVEI HGKDLVPRVY EMTTRRAVEA IAKFLGLETP
INFEEIDEKY KKVQEIVPPR PPSLCPACPH RNTFFALRKA ATPRAIYPSD IGCYTLGVLP
PLKTVDTTIA MGGSIGVAHG LSIALNGSIA EEQRKTGKGK KIIAATIGDS TFFHTGLPAL
ANAIYNRSNV LIVVLDNLVT AMTGDQPNPG TGETPHGPGK RILIEEVAKA MGADFVAVVD
PYDIKETYET FKKALEVEGV SVVVARRACA LYRIGQLRRA GKQWPIYQVN EDKCTGCKIC
INAYGCPAIY WDPEKKKAKV DPLMCWGCGG CAQVCPFDAF EKVREGEL
