(data stored in ACNUC7421 zone)

SWISSPROT: C1AT22_RHOOB

ID   C1AT22_RHOOB            Unreviewed;       404 AA.
AC   C1AT22;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
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   ECO:0000313|EMBL:BAH48954.1};
GN   OrderedLocusNames=ROP_07070 {ECO:0000313|EMBL:BAH48954.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48954.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48954.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48954.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH48954.1; -; Genomic_DNA.
DR   RefSeq; WP_012687954.1; NC_012522.1.
DR   EnsemblBacteria; BAH48954; BAH48954; ROP_07070.
DR   KEGG; rop:ROP_07070; -.
DR   PATRIC; fig|632772.20.peg.768; -.
DR   eggNOG; ENOG4108ZQD; Bacteria.
DR   eggNOG; COG0237; LUCA.
DR   eggNOG; COG2320; LUCA.
DR   HOGENOM; HOG000020768; -.
DR   KO; K00859; -.
DR   OMA; IRVDGWP; -.
DR   OrthoDB; 1515383at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000002212; 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; IPR007344; GrpB/CoaE.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   Pfam; PF04229; GrpB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AT22.
DR   SWISS-2DPAGE; C1AT22.
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:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:BAH48954.1};
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:BAH48954.1}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00376}.
SQ   SEQUENCE   404 AA;  43426 MW;  EDE2D787E58E99D9 CRC64;
     MLRIGLTGGI GAGKSTVSKV LAELGAVIVD ADLIAREVVE PGTQGLAALV DRFGEEILTA
     DGALDRPALA ARAFADEESR LALNSIVHPL VGARTTETIE SAPEDAVLVQ DIPLLVEGGM
     GAAFHLVVVV FVDAEDRVRR LVGSRGMSES DARARIAAQA DDDQRRAAAD VRLDNSGAPG
     ALEPEVRALW AERLVPFESN IRTRTVVRVL PELASPNPQW PAQADRLIAR LRLVCGDRAV
     RIDHIGSTAV EGLPAKDVID VQVTVANLEV ADELAESLAA AGFPRIEHIT ADDPKPAYQG
     GETDPALWGK RIHGGADPGR PVNIHLRVDG WPGQQFALVF RDWLRADTDA RAEYLAVKEA
     AAEKAAGHAD YQDAITAYVD AKTPWFDRAY HRAWQWAEQT GWSA
//

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