ID   COAD_MYCA9              Reviewed;         161 AA.
AC   B1MDL6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MAB_3259c;
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM63335.1; -; Genomic_DNA.
DR   RefSeq; WP_005056942.1; NZ_MLCG01000001.1.
DR   PDB; 5O06; X-ray; 1.55 A; A/B/C=1-161.
DR   PDB; 5O08; X-ray; 1.55 A; A/B/C=1-161.
DR   PDB; 5O0A; X-ray; 1.80 A; A/B/C=1-161.
DR   PDB; 5O0B; X-ray; 1.74 A; A/B/C=1-161.
DR   PDB; 5O0C; X-ray; 1.64 A; A/B/C=1-161.
DR   PDB; 5O0D; X-ray; 1.54 A; A/B/C=1-161.
DR   PDB; 5O0F; X-ray; 1.70 A; A/B/C=1-161.
DR   PDB; 5O0H; X-ray; 1.60 A; A/B/C=1-161.
DR   PDBsum; 5O06; -.
DR   PDBsum; 5O08; -.
DR   PDBsum; 5O0A; -.
DR   PDBsum; 5O0B; -.
DR   PDBsum; 5O0C; -.
DR   PDBsum; 5O0D; -.
DR   PDBsum; 5O0F; -.
DR   PDBsum; 5O0H; -.
DR   AlphaFoldDB; B1MDL6; -.
DR   SMR; B1MDL6; -.
DR   EnsemblBacteria; CAM63335; CAM63335; MAB_3259c.
DR   GeneID; 66968682; -.
DR   KEGG; mab:MAB_3259c; -.
DR   OMA; EFQMALM; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000007137; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..161
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_1000096815"
FT   BINDING         9..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         88..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           15..27
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:5O0H"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   TURN            58..60
FT                   /evidence="ECO:0007829|PDB:5O0H"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           92..109
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           127..135
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:5O0D"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:5O0D"
SQ   SEQUENCE   161 AA;  17373 MW;  B441FDDF09C11ACF CRC64;
     MTGAVCPGSF DPVTLGHLDV FERAAAQFDE VIVAVLINPN KAGMFTVDER IEMIRESTAD
     LPNLRVESGQ GLLVDFVRER GLNAIVKGLR TGTDFEYELQ MAQMNKHIAG VDTFFVATAP
     AYSFVSSSLA KEVATYGGDV SALLPASVHQ RLLGKLRGQA Q