(data stored in SCRATCH zone)

SWISSPROT: C1ARF9_RHOOB

ID   C1ARF9_RHOOB            Unreviewed;       423 AA.
AC   C1ARF9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Putative GTP cyclohydrolase II {ECO:0000313|EMBL:BAH48636.1};
DE            EC=3.5.4.25 {ECO:0000313|EMBL:BAH48636.1};
GN   OrderedLocusNames=ROP_03890 {ECO:0000313|EMBL:BAH48636.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48636.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48636.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48636.1,
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   -!- 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; AP011115; BAH48636.1; -; Genomic_DNA.
DR   RefSeq; WP_012687643.1; NC_012522.1.
DR   STRING; 632772.ROP_03890; -.
DR   EnsemblBacteria; BAH48636; BAH48636; ROP_03890.
DR   KEGG; rop:ROP_03890; -.
DR   PATRIC; fig|632772.20.peg.435; -.
DR   eggNOG; ENOG4105TCV; Bacteria.
DR   eggNOG; COG0807; LUCA.
DR   HOGENOM; HOG000077582; -.
DR   OMA; VSMSDMK; -.
DR   OrthoDB; POG091H12OL; -.
DR   BioCyc; ROPA632772:GH0Q-388-MONOMER; -.
DR   Proteomes; UP000002212; 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; C1ARF9.
DR   SWISS-2DPAGE; C1ARF9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   GTP-binding {ECO:0000256|SAAS:SAAS00711691};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00711696,
KW   ECO:0000313|EMBL:BAH48636.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00711702};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00711707};
KW   Riboflavin biosynthesis {ECO:0000256|SAAS:SAAS00711711}.
FT   DOMAIN       16    202       GTP_CH_N. {ECO:0000259|Pfam:PF12471}.
FT   DOMAIN      232    378       GTP_cyclohydro2. {ECO:0000259|Pfam:
FT                                PF00925}.
SQ   SEQUENCE   423 AA;  45435 MW;  D8BEE2835529698B CRC64;
     MSAEPVAATP DNPAGHIRLT SHSGGVGAIP VHWGAPTASE RGPVVGTTTN RAHRNVIGTH
     SGSYSIYRAL AVASGALSRH HKADLTNTAP TNAVGPYPQW SEPGKIVSLD PWGATVAEVF
     AAELAAGHDI RPSIAVTKAH VILPEIMDAI QKGRLHPDGR FLLPSGAALV TKAAIEPVWH
     LPGVAERFHC SETDLRRVLF EETGGMYPEL VTRSDLEVFL PPIGGQTVYI FGDARDLADP
     AVELTARVHD ECNGSDVFGS DICTCRPYLT HAIEECIQGA QRGGVGLVAY SRKEGRALGE
     VTKFLVYNAR KRQVGGDTAD QYFARTECVA GVQDMRFQEM MPDVLHWLGV RKIHRLVSMS
     NMKYDAITGS GIEVGERVDL PADLIPADAR VEIDAKMAAG YFTPGAVPDA EELAKVKGRE
     LDE
//

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