GCH4_POLAQ
ID GCH4_POLAQ Reviewed; 272 AA.
AC A4SZK2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
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=Pnuc_1703;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34916.1; -; Genomic_DNA.
DR AlphaFoldDB; A4SZK2; -.
DR SMR; A4SZK2; -.
DR STRING; 312153.Pnuc_1703; -.
DR EnsemblBacteria; ABP34916; ABP34916; Pnuc_1703.
DR KEGG; pnu:Pnuc_1703; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_1_1_4; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000231; 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..272
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000372033"
FT SITE 159
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 272 AA; 30294 MW; 05B8FBEFE86CD2A0 CRC64;
MNPAFLKASA MPDVQSSRDE RALPIEQVGI RGVRHPLMIR SNTGNFPSVG NFEMDVALPA
HVKGTHMSRF MALLQKQDEA IDSTTVVALV RDMLPLLDAK EGHVQFTYTH FVKKAAPVSG
VESLMDYEVT WMATAKQNDA GSVEVELGLR AQVPVMSLCP CSKEISEFGA HNQRSHVTMT
VVLDTQTKMT VEDLVSAAER EASSELWGLL KRPDEKWVTE RSYSNPKFVE DLVRDVAGRL
KADTRIQSFV VDAENFESIH NHSAFARISH KK