(data stored in ACNUC7421 zone)

SWISSPROT: COAD_AERHH

ID   COAD_AERHH              Reviewed;         160 AA.
AC   A0KEN4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
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=AHA_0166;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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:
CC       Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-
CC         CoA + diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC         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; CP000462; ABK39025.1; -; Genomic_DNA.
DR   RefSeq; WP_011704185.1; NC_008570.1.
DR   RefSeq; YP_854699.1; NC_008570.1.
DR   SMR; A0KEN4; -.
DR   STRING; 380703.AHA_0166; -.
DR   EnsemblBacteria; ABK39025; ABK39025; AHA_0166.
DR   GeneID; 4487429; -.
DR   KEGG; aha:AHA_0166; -.
DR   PATRIC; fig|380703.7.peg.156; -.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   HOGENOM; HOG000006518; -.
DR   KO; K00954; -.
DR   OMA; EFQMALM; -.
DR   BioCyc; AHYD380703:G1G7B-166-MONOMER; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000000756; 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-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
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; A0KEN4.
DR   SWISS-2DPAGE; A0KEN4.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    160       Phosphopantetheine adenylyltransferase.
FT                                /FTId=PRO_1000011086.
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   160 AA;  17651 MW;  2464744143A9B995 CRC64;
     MTNKVIYPGT FDPVTNGHTD LIGRAAKLFD EVVVGVANSP SKRPLFDLDE RVQLARQVTA
     HLPNVKVVGF SGLLVDFARE QQANVLIRGL RAVSDFEYEF QLANMNRRLM PELESVFLTP
     AEENSFISST LVKEVALHGG DIRQFVDPAV AAAIKAKQTK
//

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