COAD_ACIBC
ID COAD_ACIBC Reviewed; 163 AA.
AC B2HUN5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=ACICU_00798;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC56110.1; -; Genomic_DNA.
DR RefSeq; WP_000047853.1; NZ_CP031380.1.
DR PDB; 5YH7; X-ray; 2.03 A; A=1-163.
DR PDB; 5ZZC; X-ray; 1.96 A; A=1-163.
DR PDB; 6A6D; X-ray; 2.90 A; A=1-163.
DR PDB; 6A75; X-ray; 2.75 A; A=1-163.
DR PDB; 6A7D; X-ray; 2.74 A; A=1-163.
DR PDBsum; 5YH7; -.
DR PDBsum; 5ZZC; -.
DR PDBsum; 6A6D; -.
DR PDBsum; 6A75; -.
DR PDBsum; 6A7D; -.
DR AlphaFoldDB; B2HUN5; -.
DR SMR; B2HUN5; -.
DR GeneID; 60876939; -.
DR GeneID; 66398213; -.
DR KEGG; abc:ACICU_00798; -.
DR HOGENOM; CLU_100149_0_1_6; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000008839; 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_1000096751"
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:5ZZC"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:5ZZC"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:5ZZC"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5ZZC"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5ZZC"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:5ZZC"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5ZZC"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:5ZZC"
SQ SEQUENCE 163 AA; 18456 MW; A985166582560F3A CRC64;
MSKTRVIYPG TFDPITNGHV DLVTRASRMF DEVVVAIAIG HHKNPLFSLE ERVALAQSSL
GHLSNVEFVG FDGLLVNFFK EQKATAVLRG LRAVSDFEYE FQLANMNRQL DPHFEAVFLT
PSEQYSFISS TLIREIARLK GDVTKFVPQA VVEAFERKHQ QGW
