COAD_SHIFL
ID COAD_SHIFL Reviewed; 159 AA.
AC P0A6I8; P23875;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SF3673, S4095;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45120.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19072.1; -; Genomic_DNA.
DR RefSeq; NP_709413.1; NC_004337.2.
DR RefSeq; WP_001171866.1; NZ_WPGW01000042.1.
DR AlphaFoldDB; P0A6I8; -.
DR SMR; P0A6I8; -.
DR STRING; 198214.SF3673; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03912; D-pantetheine 4'-phosphate.
DR DrugBank; DB03170; Dephospho Coenzyme A.
DR EnsemblBacteria; AAN45120; AAN45120; SF3673.
DR EnsemblBacteria; AAP19072; AAP19072; S4095.
DR GeneID; 1026203; -.
DR GeneID; 67417636; -.
DR KEGG; sfl:SF3673; -.
DR KEGG; sfx:S4095; -.
DR PATRIC; fig|198214.7.peg.4336; -.
DR HOGENOM; CLU_100149_0_1_6; -.
DR OMA; EFQMALM; -.
DR OrthoDB; 1846503at2; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
KW 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_0000156270"
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"
SQ SEQUENCE 159 AA; 17837 MW; C4D7B8715A061B91 CRC64;
MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE RVALAQQATA
HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM QLAHMNRHLM PELESVFLMP
SKEWSFISSS LVKEVARHQG DVTHFLPENV HQALMAKLA
