(data stored in ACNUC7421 zone)

HOGENOM: SHIF8_1_PE100

ID   SHIF8_1_PE100                        STANDARD;      PRT;   887 AA.
AC   SHIF8_1_PE100; Q0T886;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pyruvate dehydrogenase E1 component; EC=1.2.4 1;
DE   (SHIF8_1.PE100).
GN   Name=aceE; OrderedLocusNames=SFV_0105;
OS   SHIGELLA FLEXNERI 5 STR. 8401.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHIF8_1.PE100.
CC       Shigella flexneri 5 str. 8401, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q0T886_SHIF8
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- GENE_FAMILY: HOG000115215 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0T886; -.
DR   EMBL; CP000266; ABF02390.1; -; Genomic_DNA.
DR   RefSeq; YP_687695.1; NC_008258.1.
DR   ProteinModelPortal; Q0T886; -.
DR   SMR; Q0T886; 57-887.
DR   STRING; Q0T886; -.
DR   EnsemblBacteria; EBESCT00000096446; EBESCP00000092642; EBESCG00000095490.
DR   GeneID; 4207864; -.
DR   GenomeReviews; CP000266_GR; SFV_0105.
DR   KEGG; sfv:SFV_0105; -.
DR   eggNOG; COG2609; -.
DR   GeneTree; EBGT00050000009226; -.
DR   OMA; DRHFVVL; -.
DR   ProtClustDB; PRK09405; -.
DR   BioCyc; SFLE373384:SFV_0105-MONOMER; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
DR   InterPro; IPR004660; 2-oxoA_DH_E1.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR015941; Transketolase-like_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF00456; Transketolase_N; 2.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52922; Transketo_C_like; 1.
DR   TIGRFAMs; TIGR00759; AceE; 1.
DR   HOGENOMDNA; SHIF8_1.PE100; -.
KW   pyruvate dehydrogenase subunit E1;
KW   Complete proteome; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
SQ   SEQUENCE   887 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
     INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
     CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
     PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
     GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
     ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
     NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
     IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
     DFGALLEEQS KELSTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
     TNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
     SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
     PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
     EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
     LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
     HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
//

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