ID C5CBM7_MICLC Unreviewed; 215 AA.
AC C5CBM7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
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 ECO:0000313|EMBL:SQG49581.1};
GN OrderedLocusNames=Mlut_11180 {ECO:0000313|EMBL:ACS30624.1};
GN ORFNames=NCTC2665_02138 {ECO:0000313|EMBL:SQG49581.1};
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS30624.1, ECO:0000313|Proteomes:UP000000738};
RN [1] {ECO:0000313|EMBL:ACS30624.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS30624.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT "Complete sequence of Micrococcus luteus NCTC 2665.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX PubMed=19948807; DOI=10.1128/JB.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [3] {ECO:0000313|EMBL:SQG49581.1, ECO:0000313|Proteomes:UP000248985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG49581.1,
RC ECO:0000313|Proteomes:UP000248985};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; CP001628; ACS30624.1; -; Genomic_DNA.
DR EMBL; LS483396; SQG49581.1; -; Genomic_DNA.
DR RefSeq; WP_010078735.1; NZ_WBMF01000004.1.
DR AlphaFoldDB; C5CBM7; -.
DR STRING; 465515.Mlut_11180; -.
DR EnsemblBacteria; ACS30624; ACS30624; Mlut_11180.
DR KEGG; mlu:Mlut_11180; -.
DR PATRIC; fig|465515.4.peg.1060; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_1_1_11; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000738; Chromosome.
DR Proteomes; UP000248985; Chromosome 1.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; 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 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}; Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ACS30624.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:SQG49581.1}.
FT BINDING 22..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 215 AA; 23112 MW; 1A5F2DD67C912A7E CRC64;
MTETDPVAER PRVHVGLTGG IAAGKSAVAR VLQERGALLV DSDALARLVL EKGTDGLAAV
RDEFGDRVIT ADGELDRVEM ARIVFGDEGA RQRLNRIVHP RIRAAARRIV AEAGPDAVVV
QDVPLLVETG QADAFDLVIV VEAPLEERLR RMVEDRGMSR ADAEARIAAQ ATDEQRRAVA
DVVIVNDADL GRLASVANQV WDRFLAPDAA EPSAD
//
