COAE_ECOLI
ID COAE_ECOLI Reviewed; 206 AA.
AC P0A6I9; P36679; P75646; Q2MCG6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376, ECO:0000303|PubMed:11292795};
DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376, ECO:0000269|PubMed:11292795};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376, ECO:0000303|PubMed:11292795};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376, ECO:0000303|PubMed:11292795};
GN Synonyms=yacE; OrderedLocusNames=b0103, JW0100;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-12, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=11292795; DOI=10.1128/jb.183.9.2774-2778.2001;
RA Mishra P.K., Park P.K., Drueckhammer D.G.;
RT "Identification of yacE (coaE) as the structural gene for dephosphocoenzyme
RT A kinase in Escherichia coli K-12.";
RL J. Bacteriol. 183:2774-2778(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [6] {ECO:0007744|PDB:1N3B}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=12538896; DOI=10.1110/ps.0227803;
RA O'Toole N., Barbosa J.A., Li Y., Hung L.W., Matte A., Cygler M.;
RT "Crystal structure of a trimeric form of dephosphocoenzyme A kinase from
RT Escherichia coli.";
RL Protein Sci. 12:327-336(2003).
RN [7] {ECO:0007744|PDB:1T3H}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RA Kuzin A.P., Chen Y., Forouhar F., Edstrom W., Benach J., Vorobiev S.,
RA Acton T., Shastry R., Ma L.-C., Xia R., Montelione G., Tong L., Hunt J.;
RT "X-ray structure of dephospho-CoA kinase from E. coli Norteast Structural
RT Genomics Consortium Target ER57.";
RL Submitted (APR-2004) to the PDB data bank.
RN [8] {ECO:0007744|PDB:1VHL, ECO:0007744|PDB:1VHT, ECO:0007744|PDB:1VIY}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 2-206 IN COMPLEXES WITH ADP AND
RP BIS(5'-ADENOSYL) TRIPHOSPHATE.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
RN [9] {ECO:0007744|PDB:6ARI}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR CM078.
RA Mayclin S.J., Dranow D.M., Lorimer D., Edwards T.E.;
RT "Crystal structure of a dephospho-CoA kinase from Escherichia coli in
RT complex with inhibitor CM078.";
RL Submitted (AUG-2017) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-
CC Rule:MF_00376, ECO:0000269|PubMed:11292795}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00376,
CC ECO:0000269|PubMed:11292795};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for dephospho-CoA {ECO:0000269|PubMed:11292795};
CC KM=0.14 mM for ATP {ECO:0000269|PubMed:11292795};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:11292795};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376,
CC ECO:0000305|PubMed:11292795}.
CC -!- SUBUNIT: Monomer (PubMed:11292795, PubMed:12538896). Forms homotrimers
CC in the presence of sulfate. The trimeric form exists in solution in
CC equilibrium with the monomeric form (PubMed:12538896).
CC {ECO:0000269|PubMed:11292795, ECO:0000269|PubMed:12538896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC Rule:MF_00376, ECO:0000305}.
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DR EMBL; U00096; AAC73214.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76040.1; -; Genomic_DNA.
DR PIR; G64732; G64732.
DR RefSeq; NP_414645.1; NC_000913.3.
DR RefSeq; WP_001269520.1; NZ_STEB01000010.1.
DR PDB; 1N3B; X-ray; 1.80 A; A/B/C=1-206.
DR PDB; 1T3H; X-ray; 2.50 A; A/B/C=1-206.
DR PDB; 1VHL; X-ray; 1.65 A; A/B/C=2-206.
DR PDB; 1VHT; X-ray; 1.59 A; A/B/C=2-206.
DR PDB; 1VIY; X-ray; 1.89 A; A/B/C=2-206.
DR PDB; 6ARI; X-ray; 2.00 A; A/B=1-206.
DR PDBsum; 1N3B; -.
DR PDBsum; 1T3H; -.
DR PDBsum; 1VHL; -.
DR PDBsum; 1VHT; -.
DR PDBsum; 1VIY; -.
DR PDBsum; 6ARI; -.
DR AlphaFoldDB; P0A6I9; -.
DR SMR; P0A6I9; -.
DR BioGRID; 4261116; 230.
DR DIP; DIP-47935N; -.
DR IntAct; P0A6I9; 1.
DR STRING; 511145.b0103; -.
DR DrugBank; DB01690; Bis(Adenosine)-5'-Triphosphate.
DR jPOST; P0A6I9; -.
DR PaxDb; P0A6I9; -.
DR PRIDE; P0A6I9; -.
DR EnsemblBacteria; AAC73214; AAC73214; b0103.
DR EnsemblBacteria; BAE76040; BAE76040; BAE76040.
DR GeneID; 949060; -.
DR KEGG; ecj:JW0100; -.
DR KEGG; eco:b0103; -.
DR PATRIC; fig|1411691.4.peg.2178; -.
DR EchoBASE; EB2218; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_1_2_6; -.
DR InParanoid; P0A6I9; -.
DR OMA; QMDIEQK; -.
DR PhylomeDB; P0A6I9; -.
DR BioCyc; EcoCyc:EG12312-MON; -.
DR BioCyc; MetaCyc:EG12312-MON; -.
DR BRENDA; 2.7.1.24; 2026.
DR SABIO-RK; P0A6I9; -.
DR UniPathway; UPA00241; UER00356.
DR EvolutionaryTrace; P0A6I9; -.
DR PRO; PR:P0A6I9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:EcoCyc.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..206
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172940"
FT DOMAIN 4..200
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376,
FT ECO:0000305|PubMed:16021622"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16021622"
FT BINDING 175..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16021622"
FT CONFLICT 72..74
FT /note="ERI -> DGL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="A -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:1VHT"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1VHT"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1VIY"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 78..102
FT /evidence="ECO:0007829|PDB:1VHT"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1VHT"
FT TURN 113..119
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1VHT"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:1VHT"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1VHT"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1VHL"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:1VHT"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1VHT"
SQ SEQUENCE 206 AA; 22622 MW; 41C69353B4EFF871 CRC64;
MRYIVALTGG IGSGKSTVAN AFADLGINVI DADIIARQVV EPGAPALHAI ADHFGANMIA
ADGTLQRRAL RERIFANPEE KNWLNALLHP LIQQETQHQI QQATSPYVLW VVPLLVENSL
YKKANRVLVV DVSPETQLKR TMQRDDVTRE HVEQILAAQA TREARLAVAD DVIDNNGAPD
AIASDVARLH AHYLQLASQF VSQEKP
