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Database: UniProt
Entry: H8YXC4_9GAMM
LinkDB: H8YXC4_9GAMM
Original site: H8YXC4_9GAMM 
ID   H8YXC4_9GAMM            Unreviewed;       540 AA.
AC   H8YXC4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=Thi970DRAFT_00752 {ECO:0000313|EMBL:EIC23100.1};
OS   Thiorhodovibrio frisius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodovibrio.
OX   NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC23100.1, ECO:0000313|Proteomes:UP000002964};
RN   [1] {ECO:0000313|Proteomes:UP000002964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EIC23100.1, ECO:0000313|Proteomes:UP000002964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=970 {ECO:0000313|EMBL:EIC23100.1,
RC   ECO:0000313|Proteomes:UP000002964};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA   Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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       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};
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC       {ECO:0000256|ARBA:ARBA00011238}.
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DR   EMBL; JH603168; EIC23100.1; -; Genomic_DNA.
DR   RefSeq; WP_009147185.1; NZ_JH603168.1.
DR   AlphaFoldDB; H8YXC4; -.
DR   STRING; 631362.Thi970DRAFT_00752; -.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_017727_0_0_6; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000002964; 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   CDD; cd02008; TPP_IOR_alpha; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF7; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 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.
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:EIC23100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002964};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          21..179
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          363..511
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   540 AA;  58387 MW;  F3DD17591FE270FD CRC64;
     MTDSLTESRQ LLSGDDAVAL AALHAGTTLG VGYPGTPSTE ILETFDRLGG RAQWSPNEKT
     ALEVGIGVAF AGARSLVTMK HVGLNVAADP LFTATYTDVD GGLVIVSADD PGMASSQNEQ
     DNRRYARAAG IPMLEPVDSQ QAYDFTWLGF ELSERWKIPV MLRLTTRVCH SLTPVQPRAP
     IPPKAVKFRR DVPARVMIPA YAKPAHHRLR TKLAEIAAWN EAEGPMETEM GSKTLGIIST
     GISAMHAREA APEASHFTFG LTYPLPITRI REFAQQFERV LVVEEGDPVL VEELRTAGIP
     VEGKTERFRF GELDVARVHR IVTGDDSEEP AQPKGKPPEL CPGCSHRNVF HALRELDCIV
     AGDIGCYTLG VLPPFSAMDT CVCMGASITT GLGLRHALPE VQARRVVSVI GDSTFVHSGL
     TGLAEMAYNP PETGHLVMIL DNETTAMTGQ QEHPGTGRSL NHERADRMDF EAVGRALGIA
     YVELIDESAK NVDLKARIAD CLARNETALM IVRQPCVLAA PKIRLYEKAA DQQCAAAPAG
//
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