(data stored in SCRATCH zone)

SWISSPROT: A8FQB2_SHESH

ID   A8FQB2_SHESH            Unreviewed;       201 AA.
AC   A8FQB2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 71.
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=Ssed_0422 {ECO:0000313|EMBL:ABV35035.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35035.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35035.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35035.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: ATP + 3'-dephospho-CoA = ADP + CoA.
CC       {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; CP000821; ABV35035.1; -; Genomic_DNA.
DR   RefSeq; WP_012140772.1; NC_009831.1.
DR   ProteinModelPortal; A8FQB2; -.
DR   STRING; 425104.Ssed_0422; -.
DR   EnsemblBacteria; ABV35035; ABV35035; Ssed_0422.
DR   KEGG; sse:Ssed_0422; -.
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; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP.
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; A8FQB2.
DR   SWISS-2DPAGE; A8FQB2.
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:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ABV35035.1};
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:ABV35035.1}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   201 AA;  22148 MW;  1C739CA510F965CB CRC64;
     MSKFIVGLTG GIGSGKTTVA NMFAELGVEL VDADIIAREV VEVGSKGLNE ISAHFGNTIL
     NKDKSLNRAT LRELIFSQPD ERQWLNDLMH PMIRSKILKC IESTTSPYAI LVAPLLFENG
     LDRLVNLSLL VDISPEQQLD RTIDRDSVSS EQIKNIIDSQ APRAERLSKA DDVIDNHGKI
     SALKGKVITL HNNYLKLANN T
//

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