GCH4_HYDCU
ID GCH4_HYDCU Reviewed; 311 AA.
AC Q31EF8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 88.
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=Tcr_1875;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABB42465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000109; ABB42465.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q31EF8; -.
DR SMR; Q31EF8; -.
DR STRING; 317025.Tcr_1875; -.
DR EnsemblBacteria; ABB42465; ABB42465; Tcr_1875.
DR KEGG; tcx:Tcr_1875; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_0_0_6; -.
DR UniPathway; UPA00848; UER00151.
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.
FT CHAIN 1..311
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000289530"
FT SITE 150
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 311 AA; 35302 MW; A943996682D67EA6 CRC64;
MPDIACQPHQ DPQGKLNWVG MSGIELPIKI EQDSQTLTLS SQVQAYVSLD DPLSKGIHMS
RLYLILDEMG SNAPLNPASI QTLLTAFIES HQGLSQNAFV EFRFDYYERR RSLKSDNSGW
KHYPCTLRGE MRNGQFECEI SISVPYSSTC PCSAALSRQL IQEAFEQQFN GQDLDYNQVL
EWLGTPEGIC ATPHSQRSYA QVKLKVNAEH PLNLSNVINQ IEDAVKTPVQ STVKREDEQE
FARLNATNLM FCEDAARRLQ AKLESCPEYK DYWVRVNHLE SLHPHDAVAI VTKNVPGGYS
DEPNFMERFQ N
