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Database: UniProt
Entry: A0A2V5L255_9MICC
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ID   A0A2V5L255_9MICC        Unreviewed;       366 AA.
AC   A0A2V5L255;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000256|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000256|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000256|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000256|HAMAP-Rule:MF_00376};
GN   ORFNames=CVV68_18920 {ECO:0000313|EMBL:PYI65285.1};
OS   Arthrobacter livingstonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI65285.1, ECO:0000313|Proteomes:UP000247832};
RN   [1] {ECO:0000313|EMBL:PYI65285.1, ECO:0000313|Proteomes:UP000247832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LI2 {ECO:0000313|EMBL:PYI65285.1,
RC   ECO:0000313|Proteomes:UP000247832};
RA   Liu Q., Xin Y.-H.;
RT   "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT   and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT   glacialis sp. nov.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00376}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the UPF0157 (GrpB)
CC       family. {ECO:0000256|ARBA:ARBA00011058}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CoaE family.
CC       {ECO:0000256|ARBA:ARBA00008826}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PYI65285.1}.
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DR   EMBL; QJVD01000027; PYI65285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5L255; -.
DR   SMR; A0A2V5L255; -.
DR   OrthoDB; 9812943at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000247832; Unassembled WGS sequence.
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   CDD; cd02022; DPCK; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR007344; GrpB/CoaE.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   PANTHER; PTHR10695:SF46; DEPHOSPHO-COA KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   Pfam; PF04229; GrpB; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00376};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:PYI65285.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   366 AA;  37657 MW;  4A5A68C987B13090 CRC64;
     MLSIGLTGGI ASGKSLLSAR FRELGAVVID ADRLARDVVA PGTPGLAAVA AGFGPAVLLR
     DGSLDRPALG AVVFADKARL AALNAIVHPL VRAAAAQLKD DAGPDAIVVQ DIPLLAETGQ
     GPNFHLVVVV DAPEDQRLAR MVGNRGMTAV DAAARMAAQA GPEQRLAAAD VVIDNSGAPE
     LALAALDALW EGRLLPFARN LAAGRPAPLA GPPSIAEPDP SWPAQAARLA ARIELAAGDA
     AVAVDHIGST SVPGLAAKDV IDFQLRVRSW ADADSVAAAL GAAGFPRRGG QWWDTGHDLA
     GGAGGERWQK RFHSAADPGR AVNLHVRVDG SPAALLALAF RDWLRSDDGA RSGYEAMLRR
     LDSPTK
//
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