(data stored in ACNUC7421 zone)

SWISSPROT: COAD_SHESH

ID   COAD_SHESH              Reviewed;         158 AA.
AC   A8FPF5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 66.
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=Ssed_0115;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34728.1; -; Genomic_DNA.
DR   RefSeq; WP_012004254.1; NC_009831.1.
DR   ProteinModelPortal; A8FPF5; -.
DR   SMR; A8FPF5; -.
DR   STRING; 425104.Ssed_0115; -.
DR   EnsemblBacteria; ABV34728; ABV34728; Ssed_0115.
DR   KEGG; sse:Ssed_0115; -.
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; UP000002015; 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; A8FPF5.
DR   SWISS-2DPAGE; A8FPF5.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    158       Phosphopantetheine adenylyltransferase.
FT                                /FTId=PRO_1000076789.
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   158 AA;  17443 MW;  C516B90B06508948 CRC64;
     MHTRAIYPGT FDPVTNGHAD LIERAAKLFK HVVIGIAANP SKKPRFTLEE RVALLQLVTS
     HLDNVEVVGF SGLLVDFAKE QKASVLVRGL RAVSDFEYEF QLANMNRRLS SDLESVFLTP
     AEENSFISST LVKEVAHHGG DVSQFVHPEV AKALMTNV
//

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