ID A0A483CNY6_9EURY Unreviewed; 590 AA.
AC A0A483CNY6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 02-APR-2025, entry version 20.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|PIRNR:PIRNR006439};
DE Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE EC=1.2.7.8 {ECO:0000256|PIRNR:PIRNR006439};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|PIRNR:PIRNR006439};
GN Name=iorA {ECO:0000313|EMBL:TAJ44312.1};
GN ORFNames=CUJ86_08880 {ECO:0000313|EMBL:TAJ44312.1};
OS Methanofollis fontis.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX NCBI_TaxID=2052832 {ECO:0000313|EMBL:TAJ44312.1, ECO:0000313|Proteomes:UP000292580};
RN [1] {ECO:0000313|EMBL:TAJ44312.1, ECO:0000313|Proteomes:UP000292580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FWC-SCC2 {ECO:0000313|EMBL:TAJ44312.1,
RC ECO:0000313|Proteomes:UP000292580};
RA Teng N.-H., Lai M.-C., Chen S.-C.;
RT "Isolation and Characterization of Methanofollis Species from Methane Seep
RT Offshore SW Taiwan.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] + CoA =
CC (indol-3-yl)acetyl-CoA + 2 reduced [2Fe-2S]-[ferredoxin] + CO2 +
CC H(+); 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|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|PIRNR:PIRNR006439}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TAJ44312.1}.
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DR EMBL; PGCL01000003; TAJ44312.1; -; Genomic_DNA.
DR RefSeq; WP_130647367.1; NZ_PGCL01000003.1.
DR AlphaFoldDB; A0A483CNY6; -.
DR OrthoDB; 19071at2157; -.
DR Proteomes; UP000292580; Unassembled WGS sequence.
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:UniProtKB-ARBA.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR FunFam; 3.40.50.970:FF:000039; Indolepyruvate oxidoreductase subunit IorA; 1.
DR Gene3D; 3.30.70.20; -; 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 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; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
KW Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-
KW 50};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006439,
KW ECO:0000256|PIRSR:PIRSR006439-50};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW Pyruvate {ECO:0000313|EMBL:TAJ44312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000292580};
KW Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 532..560
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 561..589
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 541
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 544
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 547
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 552
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 569
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 572
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 575
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 579
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ SEQUENCE 590 AA; 63166 MW; 3228804343167254 CRC64;
MVKQYLLGNE AIAHACCEAG IDCATGYPGT PSSEVIDTLR AQKDRDFYIE WSVNEKVAFE
NALAASWCGQ RSLVTMKHVG LNVAADPLMT SAYTGVKGGF VILSADDPFA HSSQNEQDTR
RYAHFAKIPC MNPSSVQEAH DMMKDAFSLS EQTGLPVIFR PTTRICHSKG DVELGKIADD
HRIGAFEKDP RQYVVIPAHT RVLHRILNEK QPMVRKAVMD LGYNTAEVRG EMAVVASGIA
AAYATEVLPP DVSLMKIGCF PIDSEWMEEF VQQHRLVLVL EEGAPIVEER LRQLSCGVEV
HGQMNGAVPK EGELSPAAAA EAMVRAKILS SSPFSAPAPA EGLPPRPPIL CAGCAHRAMF
YAIKRVFPDG IFPSDIGCYT LGLQLGTVDT TICMGASVTV GSGIAHSGEK RPVVATIGDS
TFLHTGVQGL LNAVYNDADM TLVVLDNRIT AMTGHQPNPC TGKTAMGEPS VPISLEALCR
ACGASFVETV DPYDLQGTME TLKTARDRSG TKVIIAKQAC VITSRRSGVR RGRYVVDADL
CTACGACLRF GCPAIGKDGD EKAEINDLCS GCGVCAAICP AGAIRKEGRK
//
