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Database: UniProt
Entry: K6W5X6_9MICO
LinkDB: K6W5X6_9MICO
Original site: K6W5X6_9MICO 
ID   K6W5X6_9MICO            Unreviewed;       397 AA.
AC   K6W5X6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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:GAB77227.1};
GN   ORFNames=AUCHE_05_01320 {ECO:0000313|EMBL:GAB77227.1};
OS   Austwickia chelonae NBRC 105200.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Austwickia.
OX   NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77227.1, ECO:0000313|Proteomes:UP000008495};
RN   [1] {ECO:0000313|EMBL:GAB77227.1, ECO:0000313|Proteomes:UP000008495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77227.1,
RC   ECO:0000313|Proteomes:UP000008495};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL   Submitted (AUG-2012) 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:GAB77227.1}.
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DR   EMBL; BAGZ01000005; GAB77227.1; -; Genomic_DNA.
DR   RefSeq; WP_006501979.1; NZ_BAGZ01000005.1.
DR   AlphaFoldDB; K6W5X6; -.
DR   STRING; 100225.SAMN05421595_1042; -.
DR   eggNOG; COG0237; Bacteria.
DR   eggNOG; COG2320; Bacteria.
DR   OrthoDB; 9812943at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000008495; 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:GAB77227.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000008495};
KW   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   397 AA;  43583 MW;  9E562A80EE286CFC CRC64;
     MLHVGLTGGI GSGKSTVARR LAQHGAVVID ADALAREVVS PGTSGLEQVR LRFGDDVIGP
     HGELDRRALA SIVFDDEKAR ADLESITHPL VAARTAELLA TTGEQSIVVH DVPLLVENHL
     GPDYHLVVVV EASPETRVQR LTGLRGMPEA DALARMAHQA GDEQRTAAAD VVLGNDGSLE
     QLEAAVDQLW AERLSPYEEN LWQGRLHVQQ DLPVTSSYKD EWPQQAERVI ERLSRILGAR
     APELEHVGST SVPGMPGKDV IDIQIGVTDL RSADDPEFVE ALARAGFPRV DKIRMDHPTG
     ELLDPSLWVK RFHGSCDPGR IVHIHVREAD SAGWQSALLF RDWLRANPDA ADEYVEVKNA
     LSAQSDSARA YADAKEPWFE EIWPRITAWA QKTGWRS
//
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