COAD_ACIBS
ID COAD_ACIBS Reviewed; 163 AA.
AC B0VTH7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=ABSDF2584;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 6-163, AND SUBUNIT.
RA Singh P.K., Gupta A., Kaur P., Sharma S., Singh T.P.;
RT "Crystal structure of the complex of phosphopantetheine adenylyltransferase
RT from Acinetobacter baumannii with 2-hydroxy-1,2,3-propane tricarboxylate at
RT 1.76 A resolution.";
RL Submitted (NOV-2016) to the PDB data bank.
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 ECO:0000269|Ref.2}.
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; CU468230; CAP01892.1; -; Genomic_DNA.
DR PDB; 5H16; X-ray; 2.30 A; A/B/C/D/E/F=1-163.
DR PDB; 5H7X; X-ray; 1.76 A; A/B/C/D/E/F=1-163.
DR PDB; 5YRR; X-ray; 2.88 A; A=1-163.
DR PDB; 5Z1M; X-ray; 1.87 A; A/B/C=1-163.
DR PDBsum; 5H16; -.
DR PDBsum; 5H7X; -.
DR PDBsum; 5YRR; -.
DR PDBsum; 5Z1M; -.
DR AlphaFoldDB; B0VTH7; -.
DR SMR; B0VTH7; -.
DR EnsemblBacteria; CAP01892; CAP01892; ABSDF2584.
DR KEGG; abm:ABSDF2584; -.
DR HOGENOM; CLU_100149_0_1_6; -.
DR OMA; EFQMALM; -.
DR BRENDA; 2.7.7.3; 98.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000001741; 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..163
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_1000096752"
FT BINDING 11..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 90..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:5Z1M"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:5Z1M"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5YRR"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5Z1M"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5Z1M"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:5Z1M"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5Z1M"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5Z1M"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:5Z1M"
SQ SEQUENCE 163 AA; 18387 MW; A78B0CD583FD1531 CRC64;
MSKTSVIYPG TFDPITNGHV DLVTRASRMF DEVVVAIAIG HHKNPLFSLE ERVALAQSSL
GHLSNVEFVG FDGLLVNFFK EQKATAVLRG LRAVSDFEYE FQLANMNRQL DPHFEAVFLT
PSEQYSFISS TLIREIARLK GDVTKFVPQA VVEAFERKHQ QGW
