COAD_KLEPN
ID COAD_KLEPN Reviewed; 159 AA.
AC Q9XC89;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
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}; Synonyms=kdtB;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C3;
RX PubMed=11371519; DOI=10.1128/jb.183.12.3564-3573.2001;
RA Regue M., Climent N., Abitiu N., Coderch N., Merino S., Izquierdo L.,
RA Altarriba M., Tomas J.M.;
RT "Genetic characterization of the Klebsiella pneumoniae waa gene cluster,
RT involved in core lipopolysaccharide biosynthesis.";
RL J. Bacteriol. 183:3564-3573(2001).
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; AF146532; AAD37773.1; -; Genomic_DNA.
DR RefSeq; WP_002922501.1; NZ_WYAM01000023.1.
DR PDB; 7WGJ; X-ray; 2.59 A; A/B/C=1-159.
DR PDBsum; 7WGJ; -.
DR AlphaFoldDB; Q9XC89; -.
DR SMR; Q9XC89; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..159
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156220"
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"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:7WGJ"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:7WGJ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:7WGJ"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7WGJ"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:7WGJ"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:7WGJ"
SQ SEQUENCE 159 AA; 17663 MW; 586966F4C49F2C6D CRC64;
MSTKAIYPGT FDPITNGHID IVTRAASMFD KVVLAIAASP SKKPMFSLDE RIALAEQATA
HLVNVEVIGF SDLMANFARA QQANILIRGL RAVADFEYEM QLAHMNRHLM PTLESVFLMP
CKEWSFISSS LVKEVARHQG DVSHFLPANV HQALLNKLK
