(data stored in SCRATCH zone)

SWISSPROT: B4SHM7_STRM5

ID   B4SHM7_STRM5            Unreviewed;       895 AA.
AC   B4SHM7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   OrderedLocusNames=Smal_0365 {ECO:0000313|EMBL:ACF50070.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50070.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50070.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50070.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
CC       that catalyzes the overall conversion of pyruvate to acetyl-CoA
CC       and CO(2). {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine
CC         + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111;
CC         EC=1.2.4.1; Evidence={ECO:0000256|PIRNR:PIRNR000156};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000156,
CC         ECO:0000256|SAAS:SAAS01133295};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS01133305}.
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DR   EMBL; CP001111; ACF50070.1; -; Genomic_DNA.
DR   RefSeq; WP_004139606.1; NC_011071.1.
DR   STRING; 391008.Smal_0365; -.
DR   EnsemblBacteria; ACF50070; ACF50070; Smal_0365.
DR   KEGG; smt:Smal_0365; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; REPWFPG; -.
DR   OrthoDB; 49937at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01900-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   4: Predicted;
DR   PRODOM; B4SHM7.
DR   SWISS-2DPAGE; B4SHM7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000313|EMBL:ACF50070.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000256|SAAS:SAAS01133301}.
FT   DOMAIN      139    294       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      484    704       PDH_E1_M. {ECO:0000259|Pfam:PF17831}.
FT   METAL       233    233       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       263    263       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       265    265       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000156-1}.
SQ   SEQUENCE   895 AA;  99760 MW;  22972F811D3C53CC CRC64;
     MNWLNEVLNN DPNPVETQEW IESLKAVIDV EGSERAHQLL EGMVELTRRS GAYLPFSPTT
     EYVNTIEPQL EAKSPGNAEL EWRIRSIIRW NAMATVVRAN RKPGDLGGHI ASFASGATLY
     DVGFNHFWRA PSENHPGDLL FIQGHSAPGI YARSFLEGRI SEEQLDKFRM EVDGGGLSSY
     PHPWLMPEYW QTPTVSMGLG PLAAIYQAQF MRYLENRGLI EKSDRKVWCF IGDGESDEPE
     TLGAIALAGR EGLDNLIFVV NCNLQRLDGP VRGNGKIIQE LEGVFRGGGW NVIKLLWGGY
     WDALLAKDSD GVLKKLMMET VDGEYQNCKA FGGAYTREHF FGKYPETAAM VAGLSDDDIW
     RLNRGGHDPH KVYAAYHQAV NTKGMPTVIL AKTVKGYGMG SAGEALNPTH QTKKLDDEAV
     RHFRDRFNIP VTDAQLADGQ VPFYHPGPDS PEVQYLQERR AALGGYLPQR RRKADKTFVA
     PKLEAYERLL KSSGERSYST TMAFVQSLNI TLRDKELGPH IVPIVADEAR TFGMEGLFRQ
     IGIYAPFGQK YKPVDADQLM FYREDQSGQV LQQGISEPGA ISSWMAAGTS YSVSNVPMLP
     FYIYYSMFGF QRVGDIAWQA ADMRTRGFLL GGTAGRTTLN GEGLQHEDGF SHLVAGGIPN
     VRSYDPTFGF EVTVVLQHGT KRMMEDQVDE YYYVTLMNEN YTHPEMPEGA AEGIVKGMYL
     LTDAGKPKKG ELRVQLLGSG TILREAIAAA ELLDKDFGVT ADIWSCPSFN ELRRDGFDVE
     RANRLHPEGE QRKAYVTELL EGRQGPAIAA TDYVRAYADQ IRAFVPMSYT VLGTDGFGRS
     DTRANLRRFF EVDRYYIAHA AIAALAKEGK MTAKDVARAI KQYKIDPEKA NPVGV
//

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