ID   GCH4_IDILO              Reviewed;         308 AA.
AC   Q5R041;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-MAY-2012, entry version 43.
DE   RecName: Full=GTP cyclohydrolase folE2;
DE            EC=3.5.4.16;
GN   Name=folE2; OrderedLocusNames=IL0489;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6-
CC       (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
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; AE017340; AAV81332.1; -; Genomic_DNA.
DR   RefSeq; YP_154881.1; NC_006512.1.
DR   ProteinModelPortal; Q5R041; -.
DR   GeneID; 3173826; -.
DR   GenomeReviews; AE017340_GR; IL0489.
DR   KEGG; ilo:IL0489; -.
DR   PATRIC; 22138999; VBIIdiLoi21852_0491.
DR   eggNOG; COG1469; -.
DR   HOGENOM; HOG000247517; -.
DR   KO; K09007; -.
DR   OMA; FCEDAAR; -.
DR   ProtClustDB; PRK13674; -.
DR   BioCyc; ILOI283942:IL0489-MONOMER; -.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:EC.
DR   Gene3D; G3DSA:3.10.270.10; Uricase; 2.
DR   HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1; -.
DR   InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   InterPro; IPR002042; Uricase.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    308       GTP cyclohydrolase folE2.
FT                                /FTId=PRO_0000147711.
FT   SITE        155    155       May be catalytically important (By
FT                                similarity).
SQ   SEQUENCE   308 AA;  34233 MW;  D4CDA07CC2E8FE89 CRC64;
     MPTVMPDVAN QTQAQTEGAL DWVGMSNIEV PLMVAAAGVP ERPVAAKVEA FVNLKNPKTK
     GIHMSRLYLL LDKMSTEGEL SHDTLKQLLN DFIESHKDIS DQAFIKFDFD YHLRRKSLIS
     KKQGWKAYPV SLTGRYDAGQ LKLELSVDVP YSSTCPCSAA LARQLIQDAF SEKFAGQEQV
     DASIMHEWLG STEGIVATPH SQRSVAEVKV ALSDSVNDFP IVELIDAIEG ALKTPVQAAV
     KREDEQEFAR LNGQNLMFCE DASRRLQHQL NQMSNFRDFW LRVNHYESLH AHDAVSVTTK
     GVPGGYSA
//