(data stored in ACNUC7421 zone)

SWISSPROT: Q13E27_RHOPS

ID   Q13E27_RHOPS            Unreviewed;       199 AA.
AC   Q13E27;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=RPD_0424 {ECO:0000313|EMBL:ABE37662.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37662.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37662.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37662.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group
CC       of 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
CC       (R)-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; CP000283; ABE37662.1; -; Genomic_DNA.
DR   RefSeq; WP_011500850.1; NC_007958.1.
DR   STRING; 316057.RPD_0424; -.
DR   EnsemblBacteria; ABE37662; ABE37662; RPD_0424.
DR   KEGG; rpd:RPD_0424; -.
DR   eggNOG; ENOG4108ZQD; Bacteria.
DR   eggNOG; COG0237; LUCA.
DR   HOGENOM; HOG000020768; -.
DR   KO; K00859; -.
DR   OMA; QMDIEQK; -.
DR   OrthoDB; 1515383at2; -.
DR   BioCyc; RPAL316057:RPD_RS02180-MONOMER; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000001818; 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   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; Q13E27.
DR   SWISS-2DPAGE; Q13E27.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000256|SAAS:SAAS00779404};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ABE37662.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000256|SAAS:SAAS00779396};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000313|EMBL:ABE37662.1}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   199 AA;  21683 MW;  9C98F950097E42DF CRC64;
     MLVLGLTGSI GMGKSTTAKL FEEAGVPVYD ADATVHKIYE DEAAPAIEAA FPGTTANGKV
     DRTLLSAKVV HDTEAMKRLE QIVHPMLRSH HQNFLDDAEA SGAPIAVVDV PLLFETGGEK
     RVDAVVVVTT SPEIQRERIL ARDNMTPEKL DAILARQMPD AEKRKRADFI VDTSHGLDPV
     RAQLDEILAA AARMPRRRP
//

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