(data stored in ACNUC7421 zone)

SWISSPROT: Q0SK42_RHOJR

ID   Q0SK42_RHOJR            Unreviewed;       423 AA.
AC   Q0SK42;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   SubName: Full=GTP cyclohydrolase II {ECO:0000313|EMBL:ABG92094.1};
DE            EC=3.5.4.25 {ECO:0000313|EMBL:ABG92094.1};
GN   OrderedLocusNames=RHA1_ro00258 {ECO:0000313|EMBL:ABG92094.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92094.1, 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   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC       {ECO:0000256|SAAS:SAAS00711743}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP.
CC       {ECO:0000256|SAAS:SAAS00711745}.
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DR   EMBL; CP000431; ABG92094.1; -; Genomic_DNA.
DR   RefSeq; WP_009472814.1; NC_008268.1.
DR   ProteinModelPortal; Q0SK42; -.
DR   STRING; 101510.RHA1_ro00258; -.
DR   PRIDE; Q0SK42; -.
DR   EnsemblBacteria; ABG92094; ABG92094; RHA1_ro00258.
DR   GeneID; 4217950; -.
DR   KEGG; rha:RHA1_ro00258; -.
DR   PATRIC; fig|101510.16.peg.287; -.
DR   eggNOG; ENOG4105TCV; Bacteria.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000077582; -.
DR   OMA; VSMSDMK; -.
DR   OrthoDB; POG091H12OL; -.
DR   BioCyc; RJOS101510:GJJ1-258-MONOMER; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   InterPro; IPR022163; GTP_CH_N.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   Pfam; PF12471; GTP_CH_N; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
PE   4: Predicted;
DR   PRODOM; Q0SK42.
DR   SWISS-2DPAGE; Q0SK42.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   GTP-binding {ECO:0000256|SAAS:SAAS00711691};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00711696,
KW   ECO:0000313|EMBL:ABG92094.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00711702};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00711707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Riboflavin biosynthesis {ECO:0000256|SAAS:SAAS00711711}.
FT   DOMAIN       16    202       GTP_CH_N. {ECO:0000259|Pfam:PF12471}.
FT   DOMAIN      231    378       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
SQ   SEQUENCE   423 AA;  45424 MW;  A6C5557CC2CB239E CRC64;
     MSAESVAATP EPTGGHIRLT SHSGGVGALP IHWGAPTPSE RGPVVGTTTN RAHRNVIGTH
     SGSYSIYRAL AVASGALSRH HKADLTDTAP TNIIGPYPQW SEPGKIVSLD PWGATVAEVF
     AAELAAGHDI RPSIAVTKAH VILPEIMEAI QKGRLHPDGR FLLPSGAALV TKAAIEPVWH
     LPGVAERFHC SETDLRRVLF EETGGMYPEL VTRSDLEVFL PPIGGQTVYI FGDARDLADP
     GVELTARVHD ECNGSDVFGS DICTCRPYLT HAIEECIQGA QRGGVGLVAY SRKEGRALGE
     VTKFLVYNAR KRQVGGDTAD QYFARTECVA GVQDMRFQEM MPDVLHWLGV RKIHRLVSMS
     NMKYDAITGS GIEVGERVDL PADLIPADAR VEIDAKMAAG YFTPGAVPDA DELAKVKGRE
     LDG
//

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