GCH4_XYLFT
ID GCH4_XYLFT Reviewed; 298 AA.
AC Q87DA5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 85.
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}; OrderedLocusNames=PD_0781;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAO28649.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009442; AAO28649.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q87DA5; -.
DR SMR; Q87DA5; -.
DR EnsemblBacteria; AAO28649; AAO28649; PD_0781.
DR KEGG; xft:PD_0781; -.
DR HOGENOM; CLU_062816_0_0_6; -.
DR OMA; AKGIHMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002516; Chromosome.
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.
FT CHAIN 1..298
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000147737"
FT SITE 155
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 298 AA; 32516 MW; 147C68D489CA9086 CRC64;
MSTSIPDVAV HDSPAIAAPL RWVGMDGIVV PVQLTTADGG QHVIGRARAQ IDLPAMGVKG
IHMSRLYRLL DTYAVEPLTP VGICGLLSAM VNSHADCAST AARVDWYFDW LRRVPALVSN
DLSGWRGYPV WLRAEYSAGH VQFWLCVEVA YSSTCPCSAA LARQMLADAF LQEHVEVSAL
SPETVADWLR SNGSYATPHS QRSLARIEVA LTEQAVELGL PALVDCAERI LSTPVQAAVR
RVDEQAFARL NGANLMYVED ATRRLQHGLA IHYSAFRVHV RHLESLHPND AVASTADE