(data stored in ACNUC7421 zone)

SWISSPROT: C8VVD8_DESAS

ID   C8VVD8_DESAS            Unreviewed;       589 AA.
AC   C8VVD8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
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   OrderedLocusNames=Dtox_0045 {ECO:0000313|EMBL:ACV61008.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61008.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61008.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative
CC       decarboxylation of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + S-
CC         2-(indol-3-yl)acetyl-CoA; Xref=Rhea:RHEA:12645, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17640, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57271, ChEBI:CHEBI:57287;
CC         EC=1.2.7.8; 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
CC       has a non-standard and varying [4Fe-4S] binding motif
CC       CX(2)CX(2)CX(4-5)CP. {ECO:0000256|PIRNR:PIRNR006439,
CC       ECO:0000256|PIRSR:PIRSR006439-50};
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DR   EMBL; CP001720; ACV61008.1; -; Genomic_DNA.
DR   RefSeq; WP_012813460.1; NC_013216.1.
DR   STRING; 485916.Dtox_0045; -.
DR   EnsemblBacteria; ACV61008; ACV61008; Dtox_0045.
DR   KEGG; dae:Dtox_0045; -.
DR   eggNOG; ENOG4105BZI; Bacteria.
DR   eggNOG; COG4231; LUCA.
DR   HOGENOM; HOG000224871; -.
DR   KO; K00179; -.
DR   OMA; TFLHTGI; -.
DR   OrthoDB; 342322at2; -.
DR   BioCyc; DACE485916:G1GFV-49-MONOMER; -.
DR   Proteomes; UP000002217; 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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017721; Indolepyruvate_Fd_OxRdtase_asu.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
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; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR03336; IOR_alpha; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
DR   PRODOM; C8VVD8.
DR   SWISS-2DPAGE; C8VVD8.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-
KW   50}; Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-
KW   50};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439,
KW   ECO:0000256|PIRSR:PIRSR006439-50};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006439,
KW   ECO:0000256|PIRSR:PIRSR006439-50};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW   Pyruvate {ECO:0000313|EMBL:ACV61008.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN      527    555       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      557    586       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       536    536       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       539    539       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       542    542       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       547    547       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       566    566       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       569    569       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       572    572       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       576    576       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
SQ   SEQUENCE   589 AA;  64147 MW;  AA020673C55AE8FE CRC64;
     MKDLLSGNAA IARGAYEAGV KLGVGYPGTP STEILENFAK YEGIYAQWSP NEKVALEVGI
     GASLAGVRVL VTMKHVGVNV AADPLLTFAY TGVNGGLVLL SADDPGMHSS QNEQDNRIFA
     KFAKIPMLEP SDSQEAKDMV GLALEISEKY DTPVLLRTTT RVAHSQSMTE IGERREVIDK
     PYQKNAQKYV MVPGHGRMRR YFIENRMKDL AEYSEKTPVN FTIPGDQKIG VITSGISYQY
     VREVLPDVSV LKLGMTFPLP EQMIKDFAGQ VEKLYVVEEL EPFIEEQLKI WGIEVLGKQV
     FPSIGEFSAD LIRQKFVDEK IIDASEKIAA VPEQTAPATP VRPPVQCPGC PHRGVFYTLN
     RLKLVVTGDI GCYTLGALPP LQAMDTTVCM GASISMALGM EKAVPEMKGK TVAVIGDSTF
     FHSGITGLVD VVYNQGNSTV IILDNRTTAM TGHQENPSTG INLMGQPAPV IDIEKLARAL
     GINRVTKVDP LSLEEFKNVV QQEIAADEPS VIIAQRPCEL LVKEKAAPYV VDPDVCKGCK
     QCQRLGCPAM SFNKLEKKAV IDIITCVGCG LCVQICKHGA LRQGGERNE
//

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