GCH4_PARP8
ID GCH4_PARP8 Reviewed; 268 AA.
AC B2JP67;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Bphy_3947;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001044; ACC73070.1; -; Genomic_DNA.
DR RefSeq; WP_012403243.1; NZ_CADFGH010000005.1.
DR AlphaFoldDB; B2JP67; -.
DR SMR; B2JP67; -.
DR STRING; 391038.Bphy_3947; -.
DR EnsemblBacteria; ACC73070; ACC73070; Bphy_3947.
DR KEGG; bph:Bphy_3947; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_1_1_4; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 757842at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000001192; Chromosome 2.
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.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..268
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000372025"
FT SITE 154
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 268 AA; 30032 MW; 9F0C46D021A72010 CRC64;
MNQMNPAFVM PDVQSTVDTR QIPIQRVGVK AVRHPLTVRT PDGSAQPTVG TWNLDVHLPA
EVKGTHMSRF VALLEENKAP LDSSAFRALL TSMLEKLEAP AGRIEVSFPY FVNKTAPVSG
VQSLLDYEVS LMGDSRDGAT RLFLKVLVPV TSLCPCSKKI SQYGAHNQRS HVTINAELID
DVPVEDLIRI AEEEASCELW GLLKRPDEKF VTERAYENPK FVEDLVRDVA QRLNDDHRIV
AYVLEAENFE SIHNHSAYAV IESDKRLR