(data stored in ACNUC7421 zone)

SWISSPROT: Q0SK61_RHOJR

ID   Q0SK61_RHOJR            Unreviewed;       139 AA.
AC   Q0SK61;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 74.
DE   SubName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000313|EMBL:ABG92075.1};
DE            EC=5.3.3.2 {ECO:0000313|EMBL:ABG92075.1};
GN   OrderedLocusNames=RHA1_ro00239 {ECO:0000313|EMBL:ABG92075.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92075.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00751257};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00055300}.
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DR   EMBL; CP000431; ABG92075.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0SK61; -.
DR   STRING; 101510.RHA1_ro00239; -.
DR   PRIDE; Q0SK61; -.
DR   EnsemblBacteria; ABG92075; ABG92075; RHA1_ro00239.
DR   KEGG; rha:RHA1_ro00239; -.
DR   eggNOG; COG1443; LUCA.
DR   HOGENOM; HOG000274107; -.
DR   KO; K01823; -.
DR   OrthoDB; POG091H03FW; -.
DR   BioCyc; RJOS101510:GJJ1-239-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR   PANTHER; PTHR10885; PTHR10885; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   4: Predicted;
DR   PRODOM; Q0SK61.
DR   SWISS-2DPAGE; Q0SK61.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00055303};
KW   Isomerase {ECO:0000313|EMBL:ABG92075.1};
KW   Manganese {ECO:0000256|SAAS:SAAS00055307};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN       29    139       Nudix hydrolase. {ECO:0000259|PROSITE:
FT                                PS51462}.
SQ   SEQUENCE   139 AA;  14915 MW;  0A520EB1ED308290 CRC64;
     MSPSAELLDE AGPQVGTVAE ASVHTSATPL HLAFSAYVID PEGQGLVGRR ARWKSTWPGV
     WTNSCSGHPC PGENLPEAVA RRVDEVLGII PADITLILPD FRCRTRDPHK YVGRQYRTSL
     CSSGGYTVDD SPSTVVPAN
//

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