(data stored in SCRATCH zone)

SWISSPROT: C7PYX1_CATAD

ID   C7PYX1_CATAD            Unreviewed;       316 AA.
AC   C7PYX1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000256|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000256|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000256|HAMAP-Rule:MF_00061};
GN   OrderedLocusNames=Caci_0590 {ECO:0000313|EMBL:ACU69527.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69527.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69527.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00651852}.
CC   -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-
CC       erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-
CC       D-erythritol. {ECO:0000256|HAMAP-Rule:MF_00061,
CC       ECO:0000256|SAAS:SAAS00651860}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00651857}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001700; ACU69527.1; -; Genomic_DNA.
DR   RefSeq; WP_012784822.1; NC_013131.1.
DR   ProteinModelPortal; C7PYX1; -.
DR   STRING; 479433.Caci_0590; -.
DR   EnsemblBacteria; ACU69527; ACU69527; Caci_0590.
DR   KEGG; cai:Caci_0590; -.
DR   eggNOG; ENOG4105CTR; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; VACDALW; -.
DR   OrthoDB; POG091H00XD; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00061; IspE; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR004424; IspE.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF010376; IspE; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00154; ispE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PYX1.
DR   SWISS-2DPAGE; C7PYX1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651866};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651834, ECO:0000313|EMBL:ACU69527.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651849};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651864}.
FT   DOMAIN      104    162       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      222    296       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
FT   NP_BIND     112    122       ATP. {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     27     27       {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    154    154       {ECO:0000256|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   316 AA;  32117 MW;  5B641085C3BF4E19 CRC64;
     MSSAAYIPDE GPRPGETESV TVRVPAKVNL ALSVGPLRSD GYHDLATVFH AVGLFDEVNA
     AAADTLAVTC EGEGQVEVPL DDTNLAWRAA ELLARTVGRS PGVRLHLTKG IPVAGGMAGG
     SADAAGALVA CDALWGTGLS RDDLHVLAAQ LGSDVPFALH GGTAMGTGRG EQITPVLARG
     EFHWVFAFAH DGLSTPAVFH ELDRLREAAG EEATAPGVED ELLRALRAGD STLLGAALRN
     DLTRPATSLR PDLRATLQAG REAGALGTLL SGSGPTCAFL AADAVAAATV AAALEAAPSV
     RAVRRALGPA AGAHLL
//

If you have problems or comments...

PBIL Back to PBIL home page