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Database: UniProt
Entry: B0TFJ7_HELMI
LinkDB: B0TFJ7_HELMI
Original site: B0TFJ7_HELMI 
ID   B0TFJ7_HELMI            Unreviewed;       706 AA.
AC   B0TFJ7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|ARBA:ARBA00017710};
DE            EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|ARBA:ARBA00030514};
GN   Name=oorA {ECO:0000313|EMBL:ABZ83096.1};
GN   ORFNames=HM1_0482 {ECO:0000313|EMBL:ABZ83096.1};
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ83096.1, ECO:0000313|Proteomes:UP000008550};
RN   [1] {ECO:0000313|EMBL:ABZ83096.1, ECO:0000313|Proteomes:UP000008550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550};
RX   PubMed=18441057; DOI=10.1128/JB.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={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|PIRSR:PIRSR006439-50};
CC   -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC       {ECO:0000256|ARBA:ARBA00011238}.
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DR   EMBL; CP000930; ABZ83096.1; -; Genomic_DNA.
DR   RefSeq; WP_012281458.1; NC_010337.2.
DR   AlphaFoldDB; B0TFJ7; -.
DR   STRING; 498761.HM1_0482; -.
DR   KEGG; hmo:HM1_0482; -.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_017727_0_0_9; -.
DR   OMA; VTMKQVG; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000008550; 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   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   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF6; 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; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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|PIRSR:PIRSR006439-50};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006439-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006439-
KW   50};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006439-50};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008550};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          616..648
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          676..705
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          388..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         625
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         628
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         631
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         637
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         685
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         688
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         691
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         695
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ   SEQUENCE   706 AA;  74572 MW;  AAC766786B44EDB0 CRC64;
     MNRLAEPPRR LLMGNEAIAW GAIEAGVRVV AAYPGTPSTE VTEKILEHAA DYGIYAEWSV
     NEKVALETAI AASWAGARAM ACMKQVGLNV ASDPLMTLAY LGVKGGLVLI VADDPGPHSS
     QTEQDTRLFA RFAKLPVLDP ATPEEAREMV KAAFRLSEDL QVPVIVRPTT RTAHVCQDMS
     FSPPPLPALP LPPVRFERDP GWVILPSLSA KRHRRLNAIQ DEMRRWFLQH RLNGIAPLCG
     EDGTAGCTGN CSEDTGNVKN AGYAGHSGKA VEDLAIVAGG VAYSYVQEGL AILGVSIPVY
     KVGAPVPLPS APILDFLGNK KSVLIVEEQE PVIEEQLTVE AYRTGLCLSI IGKNSGHLPR
     EGEFSTDLLL PLLRRFVTGS IHCDRTPAAS ASPAPLTPVG QPGSAPAIST GSAVAPAPVS
     AHSLPAPPLR TPILCAGCPH RNSFYAFIQA ARSRDALFTG DIGCYTLGAM PPLGAADTII
     CMGASVAMAA GFSHIEPDRP HIAFLGDSTF FHSGIPPLIN AVYQQARMTL VVLDNRTTAM
     TGHQPHPGLG RKGTGEIAPT IDIAAVARGC GVEWVRTVDP YDIAATIAAA REALDYPGVS
     VIIARRDCVN LARRSTPYRI DAEACRRCGI CLHKFGCPAL YEVKPADKAS AALSEKNLSV
     EGAGAPTTDT GQGGKPAVAI AREKCFGCGA CAQICPWKAI SPEVAS
//
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