GCH32_HALSA
ID GCH32_HALSA Reviewed; 253 AA.
AC Q9HQS9;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=GTP cyclohydrolase III 2;
DE EC=3.5.4.29;
GN Name=gch32; OrderedLocusNames=VNG_1021C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC -!- FUNCTION: Catalyzes the formation of 2-amino-5-formylamino-6-
CC ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and
CC inorganic phosphate from GTP. Also has an independent pyrophosphate
CC phosphohydrolase activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + 3 H2O = 2-amino-5-formylamino-6-(5-phospho-D-
CC ribosylamino)pyrimidin-4(3H)-one + 2 H(+) + 2 phosphate;
CC Xref=Rhea:RHEA:22468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57258; EC=3.5.4.29;
CC -!- SIMILARITY: Belongs to the archaeal-type GTP cyclohydrolase family.
CC {ECO:0000305}.
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DR EMBL; AE004437; AAG19434.1; -; Genomic_DNA.
DR PIR; F84258; F84258.
DR RefSeq; WP_010902729.1; NC_002607.1.
DR AlphaFoldDB; Q9HQS9; -.
DR SMR; Q9HQS9; -.
DR STRING; 64091.VNG_1021C; -.
DR PaxDb; Q9HQS9; -.
DR EnsemblBacteria; AAG19434; AAG19434; VNG_1021C.
DR GeneID; 5952792; -.
DR KEGG; hal:VNG_1021C; -.
DR PATRIC; fig|64091.14.peg.781; -.
DR HOGENOM; CLU_080076_0_0_2; -.
DR InParanoid; Q9HQS9; -.
DR OMA; THVTRAN; -.
DR OrthoDB; 56576at2157; -.
DR PhylomeDB; Q9HQS9; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043740; F:GTP cyclohydrolase IIa activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_00608; GTP_cyclohydro_3; 1.
DR InterPro; IPR007839; GTP_CycHdrlase_3.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR PANTHER; PTHR42202; PTHR42202; 1.
DR Pfam; PF05165; GCH_III; 1.
DR PIRSF; PIRSF009265; GTP_cyclohydro_3; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..253
FT /note="GTP cyclohydrolase III 2"
FT /id="PRO_0000145753"
FT REGION 102..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 26375 MW; FA4F431D28E2B612 CRC64;
MAAVQIDDYG PWTTEPAPRR ETDLQALQAR LFADVADFLG GRDGYAFAGR FDNMVGAATG
IAPAAFERLQ ERIRNRYPVT VSVGIGTART PADALDAAGT ALRDAGSAQD ENRQEALSHR
SPPGFAGTPG AVTIAHFDVV DATGTYTDTV SPVRAGTEIQ GAVTTLAEYL YDTHDAVTQF
VGGDNAIAVC PEIDAGIVDD ATAHVREAAG VDFQVGVGHG DTPHDAGADA KHALETCRAT
GARVHGPWTT ADD
