(data stored in SCRATCH zone)

SWISSPROT: GCH4_PARXL

ID   GCH4_PARXL              Reviewed;         268 AA.
AC   Q13RX0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE            EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN   OrderedLocusNames=Bxeno_B0201; ORFNames=Bxe_B2826;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
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:0000255|HAMAP-
CC         Rule:MF_01527};
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC       {ECO:0000255|HAMAP-Rule:MF_01527}.
DR   EMBL; CP000271; ABE33169.1; -; Genomic_DNA.
DR   RefSeq; WP_011490545.1; NZ_CP008762.1.
DR   SMR; Q13RX0; -.
DR   STRING; 266265.Bxe_B2826; -.
DR   EnsemblBacteria; ABE33169; ABE33169; Bxe_B2826.
DR   GeneID; 4006575; -.
DR   KEGG; bxb:DR64_5155; -.
DR   KEGG; bxe:Bxe_B2826; -.
DR   PATRIC; fig|266265.5.peg.4867; -.
DR   eggNOG; ENOG4105DZA; Bacteria.
DR   eggNOG; COG1469; LUCA.
DR   HOGENOM; HOG000280679; -.
DR   KO; K09007; -.
DR   OMA; HNQRGRG; -.
DR   OrthoDB; 757842at2; -.
DR   BioCyc; BXEN266265:BXE_RS23070-MONOMER; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   PANTHER; PTHR36445; PTHR36445; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13RX0.
DR   SWISS-2DPAGE; Q13RX0.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    268       GTP cyclohydrolase FolE2.
FT                                /FTId=PRO_0000289484.
FT   SITE        154    154       May be catalytically important.
FT                                {ECO:0000255|HAMAP-Rule:MF_01527}.
SQ   SEQUENCE   268 AA;  30006 MW;  DCFBF57639836259 CRC64;
     MNQMNPAFVM PDVQSTPDTR QIPIQRVGVK AVRHPLTVRT QGGEVQPTVG TWNLDVHLPA
     DQKGTHMSRF VALLEENKAP LEPATFRTML AAMLEKLEAE AGRIEVSFPY FVNKTAPVSG
     VQSLLDYEVT LTGETRNGAT RLFLRVRVPV TSLCPCSKKI SQYGAHNQRS HVTINAELAG
     DVAVEELIRI AEEEASCELW GLLKRPDEKF VTERAYENPK FVEDLVRDVA QRLNADERIV
     AYVLEAENFE SIHNHSAYAV IERDKRAG
//

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