GCH4_JANSC
ID GCH4_JANSC Reviewed; 362 AA.
AC Q28R88;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, 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=Jann_1857;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000264; ABD54774.1; -; Genomic_DNA.
DR RefSeq; WP_011454979.1; NC_007802.1.
DR AlphaFoldDB; Q28R88; -.
DR SMR; Q28R88; -.
DR STRING; 290400.Jann_1857; -.
DR EnsemblBacteria; ABD54774; ABD54774; Jann_1857.
DR KEGG; jan:Jann_1857; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_0_1_5; -.
DR OMA; AKGIHMS; -.
DR OrthoDB; 757842at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000008326; 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.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..362
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000289494"
FT SITE 222
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 362 AA; 39886 MW; E2F9E3878234C04E CRC64;
MNVHVKTADQ TPSTVQAQDA LAILSAWASE ASADQIDALD PGIARLVRVQ AYPDLRAEYP
GDFTVDEAYR ATLPDLQNGP ASLIKGANRR IQHVGISNFR LPIRYAVQDG SEVMLETSVT
GTVSLEADQK GINMSRIMRS FYKHADASFG FDVIEAALDD YKADLGSFDA RIQMRLSYPM
KVDSLRSGLS GWQYYDIALE LVERGGVRQR IVHLDYVYSS TCPCSLELSE HARATRGQLA
TPHSQRSVAR ISVELQGQGV WFEDLIEMAR SGVPTETQVM VKREDEQAFA ELNAANPIFV
EDAARLFAEQ LQAHSGVGDF RVMASHQESL HSHDAVSLLT EGDTFAEVSL DPKLFPSLIH
VG