COAE_MYCPA
ID COAE_MYCPA Reviewed; 407 AA.
AC Q740M4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=MAP_1326;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00376};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- DOMAIN: The C-terminal UPF0157 domain is involved in the proper folding
CC of the full length enzyme. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CoaE family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UPF0157 (GrpB)
CC family. {ECO:0000305}.
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DR EMBL; AE016958; AAS03643.1; -; Genomic_DNA.
DR RefSeq; WP_003876238.1; NC_002944.2.
DR AlphaFoldDB; Q740M4; -.
DR SMR; Q740M4; -.
DR STRING; 262316.MAP_1326; -.
DR EnsemblBacteria; AAS03643; AAS03643; MAP_1326.
DR KEGG; mpa:MAP_1326; -.
DR eggNOG; COG0237; Bacteria.
DR eggNOG; COG2320; Bacteria.
DR HOGENOM; CLU_067032_0_0_11; -.
DR OMA; IRVDGWP; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000580; 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 Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF01121; CoaE; 1.
DR Pfam; PF04229; GrpB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..407
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172961"
FT DOMAIN 3..201
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT REGION 196..407
FT /note="UPF0157"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ SEQUENCE 407 AA; 44150 MW; 547C2794A4D1A63F CRC64;
MLRIGLTGGI GAGKSALSSA FAQCGAVIVD GDVIAREVVR PGTEGLAALV EAFGRDILLA
DGSLDRPALA AKAFADDAAR QTLNGIVHPL VGARRAEIIA SVPADSVVVE DIPLLVESGM
APLFPLVVIV YADVEVRLRR LVEQRGMAEA DARARIAAQA SDEQRRAVAD IWLDNSGSPA
ELVQRAQQVW NERIVPFAHN LSTRQIARAP VRLVPPDPEW PAQAQRIVNR LKTASGHRAL
RVDHVGSTAL PGDPDFAAKD VIDIQITVES LAAADELVEP LLAAGYPRLE HITADVAKPD
ARSTVERYDH TGDPALWHKR IHASADPGRP TNVHIRVDGW PGQQFALLFV DWLTADPDAR
ADYLAVKRSA EQRADGDIDA YVAVKEPWFR DAYRRAWDWA DSTGWKP