GCH4_THEMA
ID GCH4_THEMA Reviewed; 259 AA.
AC Q9WXP6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=GTP cyclohydrolase FolE2;
DE EC=3.5.4.16;
DE AltName: Full=GTP cyclohydrolase 1B;
GN Name=folE2; OrderedLocusNames=TM_0039;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17032654; DOI=10.1074/jbc.m607114200;
RA El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., Iwata-Reuyl D.,
RA de Crecy-Lagard V.;
RT "Discovery of a new prokaryotic type I GTP cyclohydrolase family.";
RL J. Biol. Chem. 281:37586-37593(2006).
CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC {ECO:0000269|PubMed:17032654}.
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:0000269|PubMed:17032654};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35133.1; -; Genomic_DNA.
DR PIR; D72425; D72425.
DR RefSeq; NP_227855.1; NC_000853.1.
DR RefSeq; WP_004082504.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WXP6; -.
DR SMR; Q9WXP6; -.
DR STRING; 243274.THEMA_04605; -.
DR EnsemblBacteria; AAD35133; AAD35133; TM_0039.
DR KEGG; tma:TM0039; -.
DR eggNOG; COG1469; Bacteria.
DR InParanoid; Q9WXP6; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 757842at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..259
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000147732"
FT SITE 143
FT /note="May be catalytically important"
FT /evidence="ECO:0000250"
SQ SEQUENCE 259 AA; 30309 MW; 89A5C0EA52EEF34D CRC64;
MKDVQNEKDP RMVPLKKVGI KDLHWPLKVI LKEDGYQSTV AQISCSVDLH REKRGIHMSR
FIEVLNKLEV ITPQIFEEIL DDLIEIMEAK RAHLEIHFPY FIWKESPVSR KKSPLKVDCF
VEAEKEKNFS FKIGVRTPVH TLCPCSKEIS DYGAHNQRAF VEITVKTRKF IWFEDLVEIA
EKNASSPLYT LLKRPDEKFV TEKAYENPRF VEDVARDVAL ELEKDPRITW YRVYVESMES
IHNHNAFACV EKGDFVLEG
