GTPC1_HELPY
ID GTPC1_HELPY Reviewed; 243 AA.
AC O25613;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=GTP cyclohydrolase 1 type 2;
DE EC=3.5.4.16 {ECO:0000269|PubMed:23825549};
DE AltName: Full=GTP cyclohydrolase I;
GN OrderedLocusNames=HP_0959;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=23825549; DOI=10.1371/journal.pone.0066605;
RA Choi H.P., Juarez S., Ciordia S., Fernandez M., Bargiela R., Albar J.P.,
RA Mazumdar V., Anton B.P., Kasif S., Ferrer M., Steffen M.;
RT "Biochemical characterization of hypothetical proteins from Helicobacter
RT pylori.";
RL PLoS ONE 8:E66605-E66605(2013).
CC -!- FUNCTION: Converts GTP to dihydroneopterin triphosphate. Is not active
CC with GDP, GMP, ATP, CTP or UTP as substrate.
CC {ECO:0000269|PubMed:23825549}.
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:0000269|PubMed:23825549};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.040 mM for GTP {ECO:0000269|PubMed:23825549};
CC Note=kcat is 2593 min(-1). {ECO:0000269|PubMed:23825549};
CC pH dependence:
CC Optimum pH is about 4.0. Activity strongly decreases above this
CC value. {ECO:0000269|PubMed:23825549};
CC Temperature dependence:
CC Optimum temperature is about 35 degrees Celsius. Activity strongly
CC decreases above this value. {ECO:0000269|PubMed:23825549};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD08001.1; -; Genomic_DNA.
DR PIR; G64639; G64639.
DR RefSeq; NP_207751.1; NC_000915.1.
DR RefSeq; WP_001229797.1; NC_018939.1.
DR AlphaFoldDB; O25613; -.
DR SMR; O25613; -.
DR IntAct; O25613; 1.
DR STRING; 85962.C694_04940; -.
DR PaxDb; O25613; -.
DR EnsemblBacteria; AAD08001; AAD08001; HP_0959.
DR KEGG; hpy:HP_0959; -.
DR PATRIC; fig|85962.47.peg.1027; -.
DR eggNOG; COG0327; Bacteria.
DR OMA; ISMHTNF; -.
DR PhylomeDB; O25613; -.
DR SABIO-RK; O25613; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR PANTHER; PTHR13799; PTHR13799; 1.
DR Pfam; PF01784; NIF3; 1.
DR SUPFAM; SSF102705; SSF102705; 1.
DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..243
FT /note="GTP cyclohydrolase 1 type 2"
FT /id="PRO_0000147311"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 102
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ SEQUENCE 243 AA; 26798 MW; 499D006A957F9AE5 CRC64;
MALVKEVLVV LNRLSPFELQ ESWDNSGLNV GSENSEFSEI VACLEITLKI ALNAPQNALI
ITHHPLIFKP LKTLNDEIYP GNILKILIQK NVSVISMHTN FDKTHLNKHF AHALLEFDGL
VEKGLMLVKE NANIEFDALV KKIKSSLGVG SLACVKSSQT IKDLAFVCGS GASMFSSLKA
QSCLITGDVK YHDAMIAQSL GISLIDATHY YSERGFALIV AEILHSFNYL VTIENFKNPL
QII
