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Database: UniProt
Entry: Q74BI8_GEOSL
LinkDB: Q74BI8_GEOSL
Original site: Q74BI8_GEOSL 
ID   Q74BI8_GEOSL            Unreviewed;       605 AA.
AC   Q74BI8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   28-JUN-2023, entry version 114.
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-2 {ECO:0000313|EMBL:AAR35429.2};
GN   OrderedLocusNames=GSU2053 {ECO:0000313|EMBL:AAR35429.2};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR35429.2, ECO:0000313|Proteomes:UP000000577};
RN   [1] {ECO:0000313|EMBL:AAR35429.2, ECO:0000313|Proteomes:UP000000577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA
RC   {ECO:0000313|Proteomes:UP000000577};
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA   Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA   Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA   Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA   Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {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|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};
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DR   EMBL; AE017180; AAR35429.2; -; Genomic_DNA.
DR   RefSeq; NP_953102.2; NC_002939.5.
DR   RefSeq; WP_010942696.1; NC_002939.5.
DR   AlphaFoldDB; Q74BI8; -.
DR   STRING; 243231.GSU2053; -.
DR   DNASU; 2686024; -.
DR   EnsemblBacteria; AAR35429; AAR35429; GSU2053.
DR   KEGG; gsu:GSU2053; -.
DR   PATRIC; fig|243231.5.peg.2089; -.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_017727_0_0_7; -.
DR   InParanoid; Q74BI8; -.
DR   OMA; ERELGMH; -.
DR   OrthoDB; 9804603at2; -.
DR   Proteomes; UP000000577; 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   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; SSF54862; 4Fe-4S ferredoxins; 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|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|PIRNR:PIRNR006439};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          545..574
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          576..605
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         554
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         557
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         560
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         566
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         585
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         588
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         591
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT   BINDING         595
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ   SEQUENCE   605 AA;  64130 MW;  464602FEB6CE8551 CRC64;
     MSERKLLLGN DAMAHGLVES GCSVVASYPG TPASEILSGV ALWRERYGVP MHVEWAVNEK
     VAFEIAYAAA QSGLRAATAM KQVGLNVASD PFMSAAYLGV TGGFVVISAD DPGPHSSQTE
     QDSRLTAMSA KVPVLDPDSP NQARELIAAG FELSEAFRVP VMLRPTTRVC HANQDILPGP
     VAPSERTAAF VKDPTRWAAT PVFRHKLHLE LEEKLAGIAA WEPTAPRLLN PGVSSGKALV
     ASGVAAAHAR EVLEDLGLRD VIPLWQVVQP YPLHTAFVER LLADYDEILV LEETTGVMEL
     QLADRHRVKG KRSGFVPEVG ELSPELVERL VAAFAGIPAA PSVAPPTGGG RRPTLCPGCP
     HRASFHAIKR AAPKGIYPSD IGCYTLGLNL GGVDTVLCMG AAVSQAAGFY HAYKLSGQVP
     DIVATIGDST FFHAGIPPLI DAVVQDARFV LVILDNATTA MTGNQPTPAL GWGAGGVPTA
     TVDMEGLVKA CGVRFCRSGE PGNLPAFTAL MKEAVAFART DGLAVVIARQ PCVVDRTYTG
     ERPPKRAVRV SDACNGCRFC TTQFECPALV YDEETKRVVV DTLVCSKCGV CVDVCPRLAI
     EEVGK
//
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