ID A0A2W1JLQ4_9CYAN Unreviewed; 202 AA.
AC A0A2W1JLQ4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_1 {ECO:0000313|EMBL:PZD71812.1};
GN Synonyms=coaE {ECO:0000256|HAMAP-Rule:MF_00376};
GN ORFNames=C1752_04504 {ECO:0000313|EMBL:PZD71812.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD71812.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD71812.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD71812.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
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 -!- 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:PZD71812.1}.
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DR EMBL; PQWO01000014; PZD71812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JLQ4; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000248857; 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; 3.40.50.300; 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:PZD71812.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000248857};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:PZD71812.1}.
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 202 AA; 22537 MW; C64275381D3D8CD9 CRC64;
MPMQRIIGLT GGIATGKTTV ADYLATQYAL PILDADHYAR EAVQPGSPIL QQICDRNGPS
ILQADGTLDR QRLGDLIFSN SEERQWLEEQ IHPFVCDRIH QILQLHLQEP IVVLVIPLLF
EAQMTHLVSE IWVVHCHPEQ QKQRLMARNQ LTPTQAEARI KSQIALTEKI AQATVALDNS
KDAATLLRQV DQAIKIAPTS GD
//
