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Database: UniProt
Entry: P65635
LinkDB: P65635
Original site: P65635 
ID   ODP2_STAAM              Reviewed;         430 AA.
AC   P65635; Q99V06;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   26-NOV-2014, entry version 70.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=E2;
GN   Name=pdhC; OrderedLocusNames=SAV1095;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}.
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DR   EMBL; BA000017; BAB57257.1; -; Genomic_DNA.
DR   RefSeq; NP_371619.1; NC_002758.2.
DR   ProteinModelPortal; P65635; -.
DR   SMR; P65635; 2-79, 126-160, 187-428.
DR   STRING; 158878.SAV1095; -.
DR   World-2DPAGE; 0002:P65635; -.
DR   PRIDE; P65635; -.
DR   EnsemblBacteria; BAB57257; BAB57257; SAV1095.
DR   GeneID; 1121072; -.
DR   KEGG; sav:SAV1095; -.
DR   PATRIC; 19562889; VBIStaAur52173_1123.
DR   eggNOG; COG0508; -.
DR   HOGENOM; HOG000281564; -.
DR   KO; K00627; -.
DR   OMA; EPLKGFH; -.
DR   OrthoDB; EOG610413; -.
DR   PhylomeDB; P65635; -.
DR   BioCyc; SAUR158878:GJJ5-1114-MONOMER; -.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Complete proteome; Glycolysis; Lipoyl; Transferase.
FT   CHAIN         1    430       Dihydrolipoyllysine-residue
FT                                acetyltransferase component of pyruvate
FT                                dehydrogenase complex.
FT                                /FTId=PRO_0000162288.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    401    401       {ECO:0000255}.
FT   MOD_RES      43     43       N6-lipoyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   430 AA;  46368 MW;  4050074CAE5ACDA4 CRC64;
     MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS PVSGTVEEVM
     VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA KEEAPAEQAP VATQTEEVDE
     NRTVKAMPSV RKYAREKGVN IKAVSGSGKN GRITKEDVDA YLNGGAPTAS NESAASATSE
     EVAETPAAPA AVSLEGDFPE TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH
     RKKFKEIAAE QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT
     DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN IGSAGGQWFT
     PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD HRQIDGATGQ NAMNHIKRLL
     NNPELLLMEG
//
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