GCH4_STAA8
ID GCH4_STAA8 Reviewed; 292 AA.
AC Q2G0L1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=SAOUHSC_00549;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (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}.
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DR EMBL; CP000253; ABD29696.1; -; Genomic_DNA.
DR RefSeq; WP_000134232.1; NZ_LS483365.1.
DR RefSeq; YP_499121.1; NC_007795.1.
DR AlphaFoldDB; Q2G0L1; -.
DR SMR; Q2G0L1; -.
DR STRING; 1280.SAXN108_0623; -.
DR EnsemblBacteria; ABD29696; ABD29696; SAOUHSC_00549.
DR GeneID; 3920828; -.
DR KEGG; sao:SAOUHSC_00549; -.
DR PATRIC; fig|93061.5.peg.494; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_1_1_9; -.
DR OMA; PCSQGMS; -.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:Q2G0L1; -.
DR Proteomes; UP000008816; 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 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..292
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000289523"
FT SITE 176
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 292 AA; 33482 MW; 22E051A090E85536 CRC64;
MTEFDLSTRE GRWKHFGSVD PIEGTKPTTK NEMTDLQSTH KDFLFEIEEV GIKNLVYPVL
VDQYQTAGTF SFSTSLTKDE KGINMSRIIE SVEKHYDNGI ELEFNTLYQV LRTLQTNMKQ
NAAGVDVSGK WFFDRYSPTT NIKAVGNADV TYGLAIDGDK VTRKELTIEA TVTTLCPCSK
EISEYSAHNQ RGVVTVKTYI NKDQDIVDDY KNKILDAMEA NASSILYPIL KRPDEKRVTE
RAYENPRFVE DLIRLIAADL VEFDWLDGFD IECRNEESIH QHDAFAKLKY RK