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
//