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 01-MAY-2013, entry version 63.
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: Binds 1 lipoyl cofactor covalently (By similarity).
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry (By similarity).
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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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; GEAFVTP; -.
DR ProtClustDB; PRK11856; -.
DR BioCyc; SAUR158878:GJJ5-1114-MONOMER; -.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:EC.
DR GO; GO:0006096; P:glycolysis; 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; E3_bd; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 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 1 76 Lipoyl-binding.
FT ACT_SITE 401 401 Potential.
FT MOD_RES 43 43 N6-lipoyllysine (By similarity).
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
//
