GCH4_STACT
ID GCH4_STACT Reviewed; 292 AA.
AC B9DKT0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Sca_0230;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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 ---------------------------------------------------------------------------
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; AM295250; CAL27143.1; -; Genomic_DNA.
DR RefSeq; WP_012664258.1; NC_012121.1.
DR AlphaFoldDB; B9DKT0; -.
DR SMR; B9DKT0; -.
DR STRING; 396513.SCA_0230; -.
DR GeneID; 60546075; -.
DR KEGG; sca:SCA_0230; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_1_1_9; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 757842at2; -.
DR BioCyc; SCAR396513:SCA_RS01175-MON; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000444; 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;
KW Hydrolase.
FT CHAIN 1..292
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_1000185157"
FT SITE 176
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 292 AA; 33182 MW; BE135A24EB2C5190 CRC64;
MSEFDLTTRE GRWRHFGSVD PIEGTKPTVK EEMTDLQSTH KDFLFEIEEV GIKNLVYPVV
IDNYQTAGTF AFSTSLTREE KGINMSRILE SVEKHYDNGL ELSFNNLEAV LHTLEKHMKQ
SSAGVDVSGK WFFNRYSPVT NIKAVGNADV TYGLAVAGDQ VTRKELTVQA TVTTLCPCSK
EISEYSAHNQ RGVITVKMYI DPSATLPTDY KEVILDAMEA NASSILYPIL KRPDEKRVTE
RAYENPRFVE DLIRLIAADL VELDWAEGFD IECRNEESIH QHDAFAKLKY RK