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 25-MAY-2022, entry version 86.
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., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT 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 + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000271; ABE33169.1; -; Genomic_DNA.
DR RefSeq; WP_011490545.1; NZ_CP008762.1.
DR AlphaFoldDB; Q13RX0; -.
DR SMR; Q13RX0; -.
DR STRING; 266265.Bxe_B2826; -.
DR EnsemblBacteria; ABE33169; ABE33169; Bxe_B2826.
DR KEGG; bxb:DR64_5155; -.
DR KEGG; bxe:Bxe_B2826; -.
DR PATRIC; fig|266265.5.peg.4867; -.
DR eggNOG; COG1469; Bacteria.
DR OMA; PCSQGMS; -.
DR OrthoDB; 757842at2; -.
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;
KW Hydrolase; Reference proteome.
FT CHAIN 1..268
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000289484"
FT SITE 154
FT /note="May be catalytically important"
FT /evidence="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