(data stored in ACNUC7421 zone)

SWISSPROT: COAE_PSEHT

ID   COAE_PSEHT              Reviewed;         210 AA.
AC   Q3IID1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 79.
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};
GN   OrderedLocusNames=PSHAa0379;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
DR   EMBL; CR954246; CAI85477.1; -; Genomic_DNA.
DR   RefSeq; WP_011327090.1; NC_007481.1.
DR   ProteinModelPortal; Q3IID1; -.
DR   SMR; Q3IID1; -.
DR   STRING; 326442.PSHAa0379; -.
DR   EnsemblBacteria; CAI85477; CAI85477; PSHAa0379.
DR   KEGG; pha:PSHAa0379; -.
DR   PATRIC; fig|326442.8.peg.363; -.
DR   eggNOG; ENOG4108ZQD; Bacteria.
DR   eggNOG; COG0237; LUCA.
DR   HOGENOM; HOG000020769; -.
DR   KO; K00859; -.
DR   OMA; LVTEIWV; -.
DR   OrthoDB; POG091H02KX; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02022; DPCK; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IID1.
DR   SWISS-2DPAGE; Q3IID1.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    210       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000243318.
FT   DOMAIN       15    210       DPCK. {ECO:0000255|HAMAP-Rule:MF_00376}.
FT   NP_BIND      20     27       ATP. {ECO:0000255|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   210 AA;  23208 MW;  4460D7768EC1D6B8 CRC64;
     MSEQAVKVTN INNWVLGLTG GIGCGKTAVS NMLEALGICV VDADIIARQV VEPGSEGLKA
     IVTHFGADIL LADGNLNRSA LRELVFSNNE HKNWLNTLLH PLIRQQIIID LNNATSPYVV
     LVAPLLFENG LDKYCNRTLL IDVPKNVQIE RTVKRDNISL EQVNSIIAAQ MSREQKQQQA
     DDILNNDRSL TLVKHDLIAL HKGYLKLALK
//

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