(data stored in ACNUC7421 zone)

SWISSPROT: GCH4_EXIS2

ID   GCH4_EXIS2              Reviewed;         301 AA.
AC   B1YHT1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   11-DEC-2019, entry version 76.
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=Exig_0229;
OS   Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001022; ACB59715.1; -; Genomic_DNA.
DR   RefSeq; WP_012369140.1; NC_010556.1.
DR   SMR; B1YHT1; -.
DR   STRING; 262543.Exig_0229; -.
DR   EnsemblBacteria; ACB59715; ACB59715; Exig_0229.
DR   KEGG; esi:Exig_0229; -.
DR   eggNOG; ENOG4105DZA; Bacteria.
DR   eggNOG; COG1469; LUCA.
DR   HOGENOM; HOG000280679; -.
DR   KO; K09007; -.
DR   OMA; PCSQGMS; -.
DR   OrthoDB; 757842at2; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000001681; 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.
DR   TIGRFAMs; TIGR00294; TIGR00294; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1YHT1.
DR   SWISS-2DPAGE; B1YHT1.
KW   Hydrolase.
FT   CHAIN           1..301
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000372028"
FT   SITE            183
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   301 AA;  34076 MW;  E87B3E9FECA72F7D CRC64;
     MSTYPVTLPT KEERHKLFGS VPPIKGTKPT EKDKMIDLQN TPKNFLFALD AVGISNVKHP
     VVIQDGETTQ ATIATFELST SLVQDRKGIN MSRLTEQLDQ YHNEGWVVTN ESLIQFAREL
     AERMEQSEGQ LTIRYPWFFT RKAPATGLSG LMNAEVWQTV SVNTETNEAT LSVGLTINVT
     TLCPCSKEIS EYSAHNQRGY VTMEASLRDE ADDFNWKQEL LDAAESNASA PLHPVLKRPD
     EKRVTEMAYE NPRFVEDMVR LIAADLYEMD PIASFFVECR NEETIHQHDA IARITFDKDA
     Q
//

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