(data stored in ACNUC7421 zone)

SWISSPROT: A0LF85_SYNFM

ID   A0LF85_SYNFM            Unreviewed;       616 AA.
AC   A0LF85;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
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=Sfum_0387 {ECO:0000313|EMBL:ABK16087.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16087.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16087.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK16087.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0387; -.
DR   EnsemblBacteria; ABK16087; ABK16087; Sfum_0387.
DR   KEGG; sfu:Sfum_0387; -.
DR   eggNOG; ENOG4105BZI; Bacteria.
DR   eggNOG; COG4231; LUCA.
DR   HOGENOM; HOG000224871; -.
DR   KO; K00179; -.
DR   OMA; VTMKQVG; -.
DR   BioCyc; SFUM335543:G1G7I-392-MONOMER; -.
DR   Proteomes; UP000001784; 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; IPR017900; 4Fe4S_Fe_S_CS.
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   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   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
DR   PRODOM; A0LF85.
DR   SWISS-2DPAGE; A0LF85.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-
KW   50}; Complete proteome {ECO:0000313|Proteomes:UP000001784};
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   ECO:0000313|EMBL:ABK16087.1}; Pyruvate {ECO:0000313|EMBL:ABK16087.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN      553    583       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      585    614       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL       563    563       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       566    566       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       569    569       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       575    575       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       594    594       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       597    597       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       600    600       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
FT   METAL       604    604       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR006439-50}.
SQ   SEQUENCE   616 AA;  66904 MW;  8443E9D8AAE35A9F CRC64;
     MTERSILLGN EAIALGLLEA ECTMAASYPG TPASEILRAL ASLKERHKLD LHLEWSINEK
     AAFEVALANS YTGRRSATIM KQVGLNVAAD PLMSAAYTGV KGGFVLISAD DPGPHSSQTE
     QDSRLIAMVA KIPVFDPSSP EEAREYARRA CALSEKHEIP VMLRPTTRVC HARQDMDLRP
     VPHPKQFPLF EKNPGRWAAT PKFRLVLHRQ LNEKLARISR DPDCAPQLVN GDALGPGTRD
     GGRACIVGSG VVTAHAQEIL GELGLWDRVP FYRLPMPYPL PESFRDDLLS SYDRILILEE
     TDPVIELQLQ NREKIFGRTT GHVPTAGELL PEVVEGILRS FLGLDPSPPV EPPAYPGRRP
     TLCAGCPHRA AFFAIKKAFP KGIYPGDIGC YTLGLNLGVV DTVLCMGASI NQAAGFYHAY
     RSARRDMPPI CATIGDSTFF HAGVPALMNA VVQGARFVLV VLDNSTTAMT GHQPTPALGR
     NLDGIPVPRL SIAELAKACG VRSVAEGDPY DFDRFLDLLK AAGRHAGAED GGVAVVIAKR
     PCLMDRNQPR TWPRLRIEVN EKCKGCDFCV KQFECPALRP RGEKEPIVID DSLCSGCGVC
     VRVCPHGALE AVSEGH
//

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