(data stored in ACNUC7421 zone)

HOGENOM: STAAN_1_PE1002

ID   STAAN_1_PE1002                       STANDARD;      PRT;   160 AA.
AC   STAAN_1_PE1002; P63819; Q99UX9;
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=Phosphopantetheine adenylyltransferase; EC=2.7.7 3;AltName:
DE   Full=Dephospho-CoA pyrophosphorylase;AltName: Full=Pantetheine-phosphate
DE   adenylyltransferase; Short=PPAT; (STAAN_1.PE1002).
GN   Name=coaD; OrderedLocusNames=SA0973;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAN_1.PE1002.
CC       Staphylococcus aureus subsp. aureus N315, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:COAD_STAAN
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and
CC       pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
CC       3'-dephospho-CoA.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 4/5.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family.
CC   -!- GENE_FAMILY: HOG000006518 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P63819; Q99UX9; -.
DR   EMBL; BA000018; BAB42221.1; -; Genomic_DNA.
DR   PIR; A89883; A89883.
DR   RefSeq; NP_374242.1; NC_002745.2.
DR   ProteinModelPortal; P63819; -.
DR   SMR; P63819; 4-160.
DR   STRING; P63819; -.
DR   EnsemblBacteria; EBSTAT00000000546; EBSTAP00000000546; EBSTAG00000000546.
DR   GeneID; 1123799; -.
DR   GenomeReviews; BA000018_GR; SA0973.
DR   KEGG; sau:SA0973; -.
DR   eggNOG; COG0669; -.
DR   GeneTree; EBGT00050000024651; -.
DR   OMA; AMSDFEY; -.
DR   ProtClustDB; PRK00168; -.
DR   BioCyc; SAUR158879:SA0973-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00151; PPAT_bact; 1; -.
DR   InterPro; IPR004821; Cyt_trans-rel.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR001980; LPS_biosynth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   TIGRFAMs; TIGR01510; CoaD_prev_kdtB; 1.
DR   TIGRFAMs; TIGR00125; Cyt_tran_rel; 1.
DR   HOGENOMDNA; STAAN_1.PE1002; -.
KW   phosphopantetheine adenylyltransferase;
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
SQ   SEQUENCE   160 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEHTIAVIPG SFDPITYGHL DIIERSTDRF DEIHVCVLKN SKKEGTFSLE ERMDLIEQSV
     KHLPNVKVHQ FSGLLVDYCE QVGAKTIIRG LRAVSDFEYE LRLTSMNKKL NNEIETLYMM
     SSTNYSFISS SIVKEVAAYR ADISEFVPPY VEKALKKKFK
//

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