GCH4_PSEAE
ID GCH4_PSEAE Reviewed; 298 AA.
AC Q9HT35;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=PA5539;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08924.1; -; Genomic_DNA.
DR PIR; H82953; H82953.
DR RefSeq; NP_254226.1; NC_002516.2.
DR RefSeq; WP_003099665.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; Q9HT35; -.
DR SMR; Q9HT35; -.
DR STRING; 287.DR97_2918; -.
DR PaxDb; Q9HT35; -.
DR PRIDE; Q9HT35; -.
DR DNASU; 877616; -.
DR EnsemblBacteria; AAG08924; AAG08924; PA5539.
DR GeneID; 877616; -.
DR KEGG; pae:PA5539; -.
DR PATRIC; fig|208964.12.peg.5805; -.
DR PseudoCAP; PA5539; -.
DR HOGENOM; CLU_062816_0_0_6; -.
DR InParanoid; Q9HT35; -.
DR OMA; AKGIHMS; -.
DR PhylomeDB; Q9HT35; -.
DR BioCyc; PAER208964:G1FZ6-5666-MON; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002438; 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.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..298
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000147719"
FT SITE 149
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 298 AA; 32416 MW; 56C9CF2B60280239 CRC64;
MNALTLPDIA RQTTTADLPL DWVGMQGIAL PVQIGGQRVA AEADAGVSLD DPQARGIHMS
RLYLALAELE QGELDLSCLR AVLQRFLDSH AGLSRRAYLR LRLAPLLRRP ALVSPLSGWK
RYPLVLDTRL EGDDFQAEVH LELTYSSTCP CSAALARQLI QERFDQDFAG QPLDHASVLA
WLGSSAGIVA TPHSQRSSAH LRIGLAEDCI GLPLEELADL GESALGTAVQ TAVKRADEQA
FALANGQNLM FCEDAVRRLH RALQGYPQAS RFSIRVVHAE SLHAHDAVAE SHWQRGAA