(data stored in ACNUC7421 zone)

HOGENOM: LEXYL1_1_PE1002

ID   LEXYL1_1_PE1002                      STANDARD;      PRT;   908 AA.
AC   LEXYL1_1_PE1002; Q6AET5;
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   (LEXYL1_1.PE1002).
GN   Name=aceE; OrderedLocusNames=Lxx12700;
OS   LEIFSONIA XYLI SUBSP. XYLI STR. CTCB07.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEXYL1_1.PE1002.
CC       Leifsonia xyli subsp. xyli str. CTCB07, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6AET5_LEIXX
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; Q6AET5; -.
DR   EMBL; AE016822; AAT89110.1; -; Genomic_DNA.
DR   RefSeq; YP_062215.1; NC_006087.1.
DR   ProteinModelPortal; Q6AET5; -.
DR   GeneID; 2938684; -.
DR   GenomeReviews; AE016822_GR; Lxx12700.
DR   KEGG; lxx:Lxx12700; -.
DR   NMPDR; fig|281090.3.peg.732; -.
DR   OMA; FRQEKSH; -.
DR   ProtClustDB; PRK09405; -.
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; LEXYL1_1.PE1002; -.
KW   pyruvate dehydrogenase subunit E1;
KW   Complete proteome; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
SQ   SEQUENCE   908 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTVNDQDPYS MSNIDSDPEE TAEWQESLDA LVAAHGHERA REIMLSLLKR SKELHLGVPM
     VPTTDYINTI SPENEPDFPG DEDIERRYRA WIRWNAAILV HRAQRPGIAV GGHISTYASS
     AALYEVGFNH FFRGQDHPGG GDQIFVQGHA SPGTYARAFL EGRLSADQLD GFRQEKSHAG
     GGLSSYPHPR LMPEFWQFPT VSMGLGPINA IYQAQLNKYL TNRGIKDASD QHVWAFLGDG
     EVDEVESRGQ LQVAANEQLD NLTFVINANL QRLDGPVRGN GKIIQELESY FRGAGWNVIK
     VIWGREWDDL LARDADGALV NLMNQTPDGD YQTYKTENGA YVRENFFGRD PRTLELVKDF
     SDDEVWNLKR GGHDYRKVYA AFKAAVEHKG QPTVIIAKTI KGYGLGPSFE GRNATHQMKK
     MTLDNLKTFR DAMRIPVTDA QLEENPYLPP YYNPGPQDEA IQYLHERRRA LGGYLPERRA
     TYTQVSLPDD SAYAIAKKGS GTQEIATTMA FVRLLKDLLR AKDFGHRIVP IIPDEARTFG
     MDAFFPNAKI YNPNGQHYTS VDRELLLAYK ESPQGQIIHV GINEAGALAA FTNVGTSYAT
     QGEPLIPVYV FYSMFGFQRT GDAIWAAGDQ MARGFMIGAT AGRTTLTGEG LQHADGHSLV
     LSNTNPAVVS YDPAYGYEIG HIVRSGLERM YGKSHPEPNV MYYLTVYNEP IVQPAEPENV
     DVDGIVRGIH KLSEGEGGGP KAQLLASGVS VPWALEAQHL LQQDWGVSAD VWSVTSWGEL
     RRDGLKAEEH NFLHPQQEKQ VPYVTRKLEG AEGPFVAVTD YMHAVPDKIR PFVPGEYATL
     GADGFGFSDT RAAARRFFKI DGPSLVVRTL ELLAAQGKVD PNAPAWAIEK YLLHDVNAGT
     TGTAGGDA
//

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