位置:首页 > 蛋白库 > COAE_MYCPA
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024