(data stored in ACNUC7421 zone)

HOGENOM: STAAS_1_PE1015

ID   STAAS_1_PE1015                       STANDARD;      PRT;   370 AA.
AC   STAAS_1_PE1015; Q6GAC1;
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 subunit alpha; EC=1.2.4
DE   1; (STAAS_1.PE1015).
GN   Name=pdhA; OrderedLocusNames=SAS1028;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MSSA476.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAS_1.PE1015.
CC       Staphylococcus aureus subsp. aureus MSSA476 chromosome, complete genome
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:ODPA_STAAS
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   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- GENE_FAMILY: HOG000281335 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6GAC1; -.
DR   EMBL; BX571857; CAG42802.1; -; Genomic_DNA.
DR   RefSeq; YP_043152.1; NC_002953.3.
DR   ProteinModelPortal; Q6GAC1; -.
DR   SMR; Q6GAC1; 8-370.
DR   STRING; Q6GAC1; -.
DR   EnsemblBacteria; EBSTAT00000023291; EBSTAP00000022458; EBSTAG00000023290.
DR   GeneID; 2864107; -.
DR   GenomeReviews; BX571857_GR; SAS1028.
DR   KEGG; sas:SAS1028; -.
DR   eggNOG; COG1071; -.
DR   GeneTree; EBGT00050000024894; -.
DR   OMA; MPIHYGC; -.
DR   ProtClustDB; CLSK873381; -.
DR   BioCyc; SAUR282459:SAS1028-MON; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; Pyrv_DH_E1_asu_subgrp-x.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
DR   HOGENOMDNA; STAAS_1.PE1015; -.
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
SQ   SEQUENCE   370 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAPKLQAQFD AVKVLNDTQS KFEMVQILDE NGNVVNEDLV PDLTDEQLVE LMERMVWTRI
     LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALEKEDYI LPGYRDVPQI IWHGLPLTEA
     FLFSRGHFKG NQFPEGVNAL SPQIIIGAQY IQAAGVAFAL KKRGKNAVAI TYTGDGGSSQ
     GDFYEGINFA AAYKAPAIFV IQNNNYAIST PRSKQTAAET LAQKAIAVGI PGIQVDGMDA
     LAVYQATKEA RDRAVAGEGP TLIETMTYRY GPHTMAGDDP TRYRTSDEDA EWEKKDPLVR
     FRKFLENKGL WNEDKENEVI ERAKADIKAA IKEADNTEKQ TVTSLMEIMY EDMPQNLAEQ
     YEIYKEKESK
//

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