ID E0RD32_PAEP6 Unreviewed; 198 AA.
AC E0RD32;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=PPE_01599 {ECO:0000313|EMBL:ADM69438.1};
OS Paenibacillus polymyxa (strain E681).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM69438.1, ECO:0000313|Proteomes:UP000002227};
RN [1] {ECO:0000313|EMBL:ADM69438.1, ECO:0000313|Proteomes:UP000002227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E681 {ECO:0000313|EMBL:ADM69438.1,
RC ECO:0000313|Proteomes:UP000002227};
RX PubMed=20851896; DOI=10.1128/JB.00983-10;
RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT Paenibacillus polymyxa E681.";
RL J. Bacteriol. 192:6103-6104(2010).
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; CP000154; ADM69438.1; -; Genomic_DNA.
DR RefSeq; WP_013309611.1; NZ_CP048794.1.
DR AlphaFoldDB; E0RD32; -.
DR KEGG; ppy:PPE_01599; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_0_0_9; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000002227; Chromosome.
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:ADM69438.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 198 AA; 21958 MW; 2D610FF391D1D128 CRC64;
MNIGLTGGIA TGKSTVSALL VAKGALLIDA DAIAREVMLP GHPVLAAVIQ HFGQAIVNSD
GTLHRKKLGE IVFGDPAQRQ ALNDITHPAI REEMRLRMEA YEREQPDKLV LADIPLMYES
GLESLYEEIM VVYVPRDIQL QRLMLRDGLT EEQAGLRLSA QMDIEQKKSL ADIVIDNSGT
QSETKRQIDQ FWQRKGLA
//
