GenomeNet

Database: UniProt
Entry: A0A0S3QSE8_THET7
LinkDB: A0A0S3QSE8_THET7
Original site: A0A0S3QSE8_THET7 
ID   A0A0S3QSE8_THET7        Unreviewed;       576 AA.
AC   A0A0S3QSE8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=TST_0455 {ECO:0000313|EMBL:BAT71263.1};
OS   Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS   ABI70S6).
OC   Bacteria; Aquificota; Aquificae; Aquificales.
OX   NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT71263.1, ECO:0000313|Proteomes:UP000063234};
RN   [1] {ECO:0000313|Proteomes:UP000063234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6
RC   {ECO:0000313|Proteomes:UP000063234};
RX   PubMed=29420286; DOI=10.1126/science.aao3407;
RA   Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA   Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA   Fujita N., Takaki Y., Atomi H., Takai K.;
RT   "A primordial and reversible TCA cycle in a facultatively
RT   chemolithoautotrophic thermophile.";
RL   Science 359:559-563(2018).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP013035; BAT71263.1; -; Genomic_DNA.
DR   RefSeq; WP_068549182.1; NZ_AP013035.1.
DR   AlphaFoldDB; A0A0S3QSE8; -.
DR   STRING; 1298851.TST_0455; -.
DR   KEGG; ttk:TST_0455; -.
DR   PATRIC; fig|1298851.3.peg.466; -.
DR   OrthoDB; 9804603at2; -.
DR   Proteomes; UP000063234; 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   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; 3.40.50.970; -; 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:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 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   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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:BAT71263.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063234};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          518..538
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          545..575
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         527
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         530
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         533
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         538
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         554
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         557
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         560
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         564
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ   SEQUENCE   576 AA;  62628 MW;  03774955FAE0E8D0 CRC64;
     MKRFLSGNEA VARGAWEAGL RFASSYPGTP ATEILQSLVQ YKEVHAEWAP NEKVALESAI
     GASFAGVRSM ASMKHVGLNV AADPFMTLAY TGVNAGLVLA VADDPGLYSS QNEQDTRNYV
     KAARILALEP SDSQEALDYT KKAFELSERY DIPVLIRLTT RISHSKSVVK VGDRIEVGQK
     EPQIEPAKWV MLPAYAKGRH LSLLERHRLL KEFVESSEAD IFFKEELLDE SVGFIASGVC
     YQYVKEAFPE ASVFKLGIIN PLPFERLKSF ADKLRKVYVV EELDPVIEEQ LKAFGLEVVG
     KEIFPENGEF TPDVVKKAVD KDYKPKYVSF NNIPARPPTL CPGCPHRGVF VALKKARVTV
     FGDIGCYTLG ALPPLSSIHS CVCMGAGVSM VHGANVAGLK KSVAIIGDST FLHSGVTSLM
     NIIYNKSTST VIIMDNGTTA MTGKQPHPGT GVNAKGEPTN KVDLEALVKT LGVKRVRVVD
     PYDVKATYEA IKEEVETEEP SVVITRRPCT LIVQRPSKGY KVDADKCISC GACMRVGCMA
     ISMNGSASID EVLCFGCGVC VQVCPVDAIS EVNNEN
//
DBGET integrated database retrieval system