(data stored in ACNUC7421 zone)

SWISSPROT: COAD_PSEAB

ID   COAD_PSEAB              Reviewed;         159 AA.
AC   Q02U51;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   05-JUL-2017, entry version 70.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE            EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151};
GN   OrderedLocusNames=PA14_04760;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and
CC       pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
CC       3'-dephospho-CoA. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00151};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family.
CC       {ECO:0000255|HAMAP-Rule:MF_00151}.
DR   EMBL; CP000438; ABJ15328.1; -; Genomic_DNA.
DR   RefSeq; WP_003084466.1; NC_008463.1.
DR   ProteinModelPortal; Q02U51; -.
DR   SMR; Q02U51; -.
DR   EnsemblBacteria; ABJ15328; ABJ15328; PA14_04760.
DR   KEGG; pau:PA14_04760; -.
DR   HOGENOM; HOG000006518; -.
DR   KO; K00954; -.
DR   OMA; EFQMALM; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02163; PPAT; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00151; PPAT_bact; 1.
DR   InterPro; IPR013166; Citrate_lyase_ligase_C.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR001980; PPAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   SMART; SM00764; Citrate_ly_lig; 1.
DR   TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02U51.
DR   SWISS-2DPAGE; Q02U51.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    159       Phosphopantetheine adenylyltransferase.
FT                                /FTId=PRO_1000011205.
FT   NP_BIND       9     10       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND      88     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND     123    129       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING       9      9       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      73     73       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      87     87       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      98     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   159 AA;  17771 MW;  E0B0293D1B007B69 CRC64;
     MNRVLYPGTF DPITKGHGDL IERASRLFDH VIIAVAASPK KNPLFSLEQR VALAQEVTKH
     LPNVEVVGFS TLLAHFVKEQ KANVFLRGLR AVSDFEYEFQ LANMNRQLAP DVESMFLTPS
     EKYSFISSTL VREIAALGGD ISKFVHPAVA DALAERFKR
//

If you have problems or comments...

PBIL Back to PBIL home page