COAE_CAMJE
ID COAE_CAMJE Reviewed; 201 AA.
AC Q9PMD9; Q0P895;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=Cj1530;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC Rule:MF_00376, ECO:0000305}.
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DR EMBL; AL111168; CAL35630.1; -; Genomic_DNA.
DR PIR; H81299; H81299.
DR RefSeq; WP_002851523.1; NC_002163.1.
DR RefSeq; YP_002344902.1; NC_002163.1.
DR PDB; 4ZO4; X-ray; 2.57 A; A/B/C/D=2-201.
DR PDBsum; 4ZO4; -.
DR AlphaFoldDB; Q9PMD9; -.
DR SMR; Q9PMD9; -.
DR IntAct; Q9PMD9; 2.
DR STRING; 192222.Cj1530; -.
DR PaxDb; Q9PMD9; -.
DR PRIDE; Q9PMD9; -.
DR EnsemblBacteria; CAL35630; CAL35630; Cj1530.
DR GeneID; 905813; -.
DR KEGG; cje:Cj1530; -.
DR PATRIC; fig|192222.6.peg.1507; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_0_0_7; -.
DR OMA; QMDIEQK; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000799; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
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; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..201
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172922"
FT DOMAIN 4..201
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 STRAND 2..11
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:4ZO4"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4ZO4"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 79..106
FT /evidence="ECO:0007829|PDB:4ZO4"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4ZO4"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:4ZO4"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4ZO4"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:4ZO4"
SQ SEQUENCE 201 AA; 23048 MW; 532D6B6C821B2608 CRC64;
MKNAFFVTAS IACGKSTFIE IANSLGFKSI SADKIAHKIL DENALELEKI FSPFSLKNLL
KKEKKIDRKI LGEIVFNNKE AKKILENFTH PKIRAKILEQ MQILDKENKA FFVEIPLFFE
SGAYENLGKV IVIYTPKELS LKRIMQRDKL SLEAAKARLD SQIDIEEKLK KADFIIKNTN
SYADFRQECV KVIQEISKGN M
