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COAE_VIBCH
ID   COAE_VIBCH              Reviewed;         202 AA.
AC   Q9KPE3; Q9X4H0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 123.
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=VC_2427;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10024587; DOI=10.1128/iai.67.3.1393-1404.1999;
RA   Fullner K.J., Mekalanos J.J.;
RT   "Genetic characterization of a new type IV-A pilus gene cluster found in
RT   both classical and El Tor biotypes of Vibrio cholerae.";
RL   Infect. Immun. 67:1393-1404(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF109904; AAD21033.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95570.1; ALT_INIT; Genomic_DNA.
DR   PIR; C82078; C82078.
DR   RefSeq; NP_232057.1; NC_002505.1.
DR   RefSeq; WP_000011557.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPE3; -.
DR   SMR; Q9KPE3; -.
DR   STRING; 243277.VC_2427; -.
DR   DNASU; 2612969; -.
DR   EnsemblBacteria; AAF95570; AAF95570; VC_2427.
DR   GeneID; 57741033; -.
DR   KEGG; vch:VC_2427; -.
DR   PATRIC; fig|243277.26.peg.2310; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_1_2_6; -.
DR   OMA; QMDIEQK; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000000584; Chromosome 1.
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; IBA:GO_Central.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 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;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..202
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000173027"
FT   DOMAIN          4..201
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   CONFLICT        72
FT                   /note="R -> C (in Ref. 1; AAD21033)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  22307 MW;  00811CBEB7C828C9 CRC64;
     MSFVVALTGG IASGKTTVAN LFHDQFGIDL VDADVIARDV VKPETEGLKA IAAHFGQAIL
     HPDGSLNRAA LRERIFAAPN EKAWLNQLLH PMIRQGMRNA LTQTTSPYAL LIVPLLVENQ
     LQTMADRVLV VDVDEKIQIE RTMARDKVSR EQAEAILAAQ ASRAQRLAIA DDVLKNDAEN
     QKLLPQITLL HQKYLAMSRQ NL
 
 
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