COAD_YERPE
ID COAD_YERPE Reviewed; 159 AA.
AC Q8ZJN9; Q0WKN9;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
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;
GN OrderedLocusNames=YPO0053, y0088, YP_0054;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RA Osipiuk J., Maltseva N., Makowska-grzyska M., Kwon K., Anderson W.F.,
RA Joachimiak A.;
RT "X-ray crystal structure of phosphopantetheine adenylyltransferase from
RT Yersinia pestis.";
RL Submitted (JAN-2010) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC Rule:MF_00151}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590842; CAL18743.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83682.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60335.1; -; Genomic_DNA.
DR PIR; AF0007; AF0007.
DR RefSeq; WP_002208988.1; NZ_WUCM01000015.1.
DR RefSeq; YP_002345149.1; NC_003143.1.
DR PDB; 3L92; X-ray; 1.89 A; A=1-159.
DR PDB; 3L93; X-ray; 2.16 A; A=1-159.
DR PDBsum; 3L92; -.
DR PDBsum; 3L93; -.
DR AlphaFoldDB; Q8ZJN9; -.
DR SMR; Q8ZJN9; -.
DR STRING; 214092.YPO0053; -.
DR PaxDb; Q8ZJN9; -.
DR DNASU; 1145035; -.
DR EnsemblBacteria; AAM83682; AAM83682; y0088.
DR EnsemblBacteria; AAS60335; AAS60335; YP_0054.
DR GeneID; 57974537; -.
DR KEGG; ype:YPO0053; -.
DR KEGG; ypk:y0088; -.
DR KEGG; ypm:YP_0054; -.
DR PATRIC; fig|1028802.3.peg.668; -.
DR eggNOG; COG0669; Bacteria.
DR HOGENOM; CLU_100149_0_1_6; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; Q8ZJN9; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..159
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156315"
FT BINDING 10..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|Ref.4, ECO:0007744|PDB:3L92"
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 ECO:0000305|Ref.4, ECO:0007744|PDB:3L92"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|Ref.4, ECO:0007744|PDB:3L92"
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 ECO:0000305|Ref.4, ECO:0007744|PDB:3L92"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|Ref.4, ECO:0007744|PDB:3L92"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000305|Ref.4"
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:3L92"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:3L92"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3L92"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:3L92"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3L92"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3L92"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3L92"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3L92"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:3L92"
SQ SEQUENCE 159 AA; 17651 MW; E4AEB364969532C0 CRC64;
MITKAIYPGT FDPITNGHLD LVTRASAMFS HVILAIADSS SKKPMFTLDE RVALAKKVTA
PLKNVEVLGF SELMAEFAKK HNANILVRGL RSVSDFEYEW QLANMNRHLM PKLESVFLIP
SEKWSFISSS LVKEVARHGG DITPFLPKPV TKALLAKLA
