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Database: UniProt
Entry: A0A0M2RWR9_9ACTN
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ID   A0A0M2RWR9_9ACTN        Unreviewed;       392 AA.
AC   A0A0M2RWR9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:KKJ99388.1};
GN   ORFNames=LQ51_22935 {ECO:0000313|EMBL:KKJ99388.1};
OS   Micromonospora sp. HK10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ99388.1, ECO:0000313|Proteomes:UP000034330};
RN   [1] {ECO:0000313|EMBL:KKJ99388.1, ECO:0000313|Proteomes:UP000034330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK10 {ECO:0000313|EMBL:KKJ99388.1,
RC   ECO:0000313|Proteomes:UP000034330};
RA   Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT   "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT   National park, Assam, India.";
RL   Submitted (NOV-2014) 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:KKJ99388.1}.
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DR   EMBL; JTGL01000180; KKJ99388.1; -; Genomic_DNA.
DR   RefSeq; WP_046571240.1; NZ_KQ058895.1.
DR   AlphaFoldDB; A0A0M2RWR9; -.
DR   STRING; 1538294.LQ51_22935; -.
DR   PATRIC; fig|1538294.3.peg.6084; -.
DR   HOGENOM; CLU_067032_0_0_11; -.
DR   OrthoDB; 9812943at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000034330; 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:KKJ99388.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:KKJ99388.1}.
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   392 AA;  42495 MW;  2F0BFD420CAC87C4 CRC64;
     MLIVGLTGGI GSGKSAVANR LAALGAVIVD SDRIAREVVA PGSAGLAEIV AAFSERVLDE
     RGALDRAALG ALVFGDEAAR RRLEAITHPR VRTRSAELIA AAPPDAVVVN DVPLLVEVGL
     APTYHLVVVV RAAVATRLER LARHRGMERA EAERRIAAQA DDARREAAAD VLLDNDGTLD
     DLAAAVDALW HDRLLPYERN VRERRAVHRA ELVLTEPDPT WPEQYARLAA RIRHAAGADL
     RVDHIGSTAV PGLAAKDVID IQLTVSSLAE ADGALGDRLA DAGFPRLPGD WWDNPRPPGS
     TRWAKRLHGS ADPGRPVHLH LRVDGSPGWR YALLMRDHLR ADPAQRAAYL QVKRELAAAA
     PDSATYGTLK DPWFDEEHLR AEEWAARTGW RP
//
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