ID   COAD_SERP5              Reviewed;         161 AA.
AC   A8GLE1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Spro_4838;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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 pyrophosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC         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 (R)-
CC       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. {ECO:0000255|HAMAP-
CC       Rule:MF_00151}.
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DR   EMBL; CP000826; ABV43931.1; -; Genomic_DNA.
DR   RefSeq; WP_012147511.1; NC_009832.1.
DR   AlphaFoldDB; A8GLE1; -.
DR   SMR; A8GLE1; -.
DR   STRING; 399741.Spro_4838; -.
DR   EnsemblBacteria; ABV43931; ABV43931; Spro_4838.
DR   KEGG; spe:Spro_4838; -.
DR   eggNOG; COG0669; Bacteria.
DR   HOGENOM; CLU_100149_0_1_6; -.
DR   OMA; EFQMALM; -.
DR   OrthoDB; 1846503at2; -.
DR   UniPathway; UPA00241; UER00355.
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;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..161
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_1000058169"
FT   BINDING         10..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         89..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
SQ   SEQUENCE   161 AA;  17792 MW;  951C28422FAB70E9 CRC64;
     MTRKAIYPGT FDPMTNGHLD LVTRASLMFD HVILAIAASP SKKPLFTLDE RVALASQVTS
     HLDNVEVLGF SELMAHFAAH QNANILVRGL RAVSDFEYEL QLANMNRHLM PTLESVFLMP
     SEEWSFISSS LVKEVARHGG DIAPFLPAVV TQALFEKLAA Q