(data stored in SCRATCH zone)

SWISSPROT: C0ZPK6_RHOE4

ID   C0ZPK6_RHOE4            Unreviewed;       205 AA.
AC   C0ZPK6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 66.
DE   RecName: Full=GTP cyclohydrolase 1 {ECO:0000256|HAMAP-Rule:MF_00223};
DE            EC=3.5.4.16 {ECO:0000256|HAMAP-Rule:MF_00223};
DE   AltName: Full=GTP cyclohydrolase I {ECO:0000256|HAMAP-Rule:MF_00223};
DE            Short=GTP-CH-I {ECO:0000256|HAMAP-Rule:MF_00223};
GN   Name=folE {ECO:0000256|HAMAP-Rule:MF_00223,
GN   ECO:0000313|EMBL:BAH31334.1};
GN   OrderedLocusNames=RER_06260 {ECO:0000313|EMBL:BAH31334.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31334.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
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-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31334.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate +
CC         formate + H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58462; EC=3.5.4.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00223, ECO:0000256|SAAS:SAAS01118752};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00223,
CC       ECO:0000256|SAAS:SAAS00021202}.
CC   -!- SUBUNIT: Homopolymer. {ECO:0000256|HAMAP-Rule:MF_00223}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC       {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00673743}.
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DR   EMBL; AP008957; BAH31334.1; -; Genomic_DNA.
DR   RefSeq; WP_019746783.1; NC_012490.1.
DR   STRING; 234621.RER_06260; -.
DR   EnsemblBacteria; BAH31334; BAH31334; RER_06260.
DR   GeneID; 31540470; -.
DR   KEGG; rer:RER_06260; -.
DR   PATRIC; fig|234621.6.peg.1072; -.
DR   eggNOG; ENOG4105EUJ; Bacteria.
DR   eggNOG; COG0302; LUCA.
DR   HOGENOM; HOG000221222; -.
DR   KO; K01495; -.
DR   OMA; IVVVECE; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00223; FolE; 1.
DR   InterPro; IPR001474; GTP_CycHdrlase_I.
DR   InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR   InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR   PANTHER; PTHR11109; PTHR11109; 1.
DR   Pfam; PF01227; GTP_cyclohydroI; 1.
DR   TIGRFAMs; TIGR00063; folE; 1.
DR   PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR   PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C0ZPK6.
DR   SWISS-2DPAGE; C0ZPK6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021177, ECO:0000313|EMBL:BAH31334.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021169};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00223};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00223,
KW   ECO:0000256|SAAS:SAAS00021243};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00223, ECO:0000256|SAAS:SAAS00021207}.
FT   DOMAIN       25    202       GTP_cyclohydroI. {ECO:0000259|Pfam:
FT                                PF01227}.
FT   METAL        93     93       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   METAL        96     96       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
FT   METAL       166    166       Zinc. {ECO:0000256|HAMAP-Rule:MF_00223}.
SQ   SEQUENCE   205 AA;  22229 MW;  8B6211C480AE54E7 CRC64;
     MSVNDVASEL VSLGTGRPFD QARAEAAVRE LLIAVGEDPE RPGLLDTPAR VARSYKEIFA
     GLYSEPDDAL NTTFDEGHQE LVLVRDIPMF STCEHHLVSF HGVAHVGYIP GKSGKVTGLS
     KLARVVDLYA KRPQVQERLT SQIADALMRK LDPRGAIVVI EAEHLCMAMR GIRKPGASTT
     TSAVRGLLQS SAASRSEALD LILRK
//

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