(data stored in ACNUC7421 zone)

SWISSPROT: COAD_EDWI9

ID   COAD_EDWI9              Reviewed;         161 AA.
AC   C5B9D9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   05-JUL-2017, entry version 54.
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=NT01EI_0058;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67318.1; -; Genomic_DNA.
DR   RefSeq; WP_015869541.1; NC_012779.2.
DR   SMR; C5B9D9; -.
DR   STRING; 634503.NT01EI_0058; -.
DR   EnsemblBacteria; ACR67318; ACR67318; NT01EI_0058.
DR   GeneID; 7959779; -.
DR   KEGG; eic:NT01EI_0058; -.
DR   PATRIC; fig|634503.3.peg.52; -.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   HOGENOM; HOG000006518; -.
DR   KO; K00954; -.
DR   OMA; EFQMALM; -.
DR   OrthoDB; POG091H01F1; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000001485; Chromosome.
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: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; 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   TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B9D9.
DR   SWISS-2DPAGE; C5B9D9.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    161       Phosphopantetheine adenylyltransferase.
FT                                /FTId=PRO_1000203419.
FT   NP_BIND      10     11       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND      89     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND     124    130       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      10     10       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      18     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      42     42       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      74     74       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      88     88       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   SITE         18     18       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   161 AA;  17847 MW;  5F92981230CB4E13 CRC64;
     MSRTAIYPGT FDPLTNGHLD IVTRAAHMFD SVILAIAASP GKQPLFTLEE RVAMAREVTA
     HLTNVEVHGF SELMAHFAQR QGANILVRGL RAVSDFEYEL QLANMNRHLM PTLESVFLMP
     AEAWSFISSS LVKEVARHGG DVDAFLPEQV ARALMTRLRD A
//

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