(data stored in ACNUC7421 zone)

SWISSPROT: A0LEL1_SYNFM

ID   A0LEL1_SYNFM            Unreviewed;       202 AA.
AC   A0LEL1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=Sfum_0161 {ECO:0000313|EMBL:ABK15863.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15863.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15863.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
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., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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; CP000478; ABK15863.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0161; -.
DR   EnsemblBacteria; ABK15863; ABK15863; Sfum_0161.
DR   KEGG; sfu:Sfum_0161; -.
DR   eggNOG; ENOG4108ZQD; Bacteria.
DR   eggNOG; COG0237; LUCA.
DR   HOGENOM; HOG000020768; -.
DR   KO; K00859; -.
DR   OMA; QMDIEQK; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000001784; 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; A0LEL1.
DR   SWISS-2DPAGE; A0LEL1.
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:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ABK15863.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000256|SAAS:SAAS00779396};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376,
KW   ECO:0000313|EMBL:ABK15863.1}.
FT   NP_BIND      12     19       ATP. {ECO:0000256|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   202 AA;  23109 MW;  34AE0CC2EF3342FB CRC64;
     MRVNAKRIAL TGGIASGKST VARMFADRGA LILDADVAAR EAVEPGSECW QRLREWLAPA
     FFDAEGRLDR RRLRDLIIRD PQCLVRLNAI LHPFIFARME SQWRREIEAR TRRVVIFDIP
     LLFESHAADR FDIVILVHVP PEIQIGRLMK RDGLTRAEAE KTLEIQLPID SKIPLSQIVI
     DNSLDLDHTS RQVLDAWNRI AS
//

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