GCH31_HALSA
ID GCH31_HALSA Reviewed; 255 AA.
AC Q9HQT7;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=GTP cyclohydrolase III 1;
DE EC=3.5.4.29;
GN Name=gch31; OrderedLocusNames=VNG_1011C;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG19426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG19426.1; ALT_INIT; Genomic_DNA.
DR PIR; F84257; F84257.
DR RefSeq; WP_010902721.1; NC_002607.1.
DR AlphaFoldDB; Q9HQT7; -.
DR SMR; Q9HQT7; -.
DR STRING; 64091.VNG_1011C; -.
DR PaxDb; Q9HQT7; -.
DR EnsemblBacteria; AAG19426; AAG19426; VNG_1011C.
DR GeneID; 5953751; -.
DR KEGG; hal:VNG_1011C; -.
DR PATRIC; fig|64091.14.peg.773; -.
DR HOGENOM; CLU_080076_0_0_2; -.
DR InParanoid; Q9HQT7; -.
DR OrthoDB; 56576at2157; -.
DR PhylomeDB; Q9HQT7; -.
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..255
FT /note="GTP cyclohydrolase III 1"
FT /id="PRO_0000145752"
SQ SEQUENCE 255 AA; 27498 MW; 97C55FE6A7A46773 CRC64;
MTNTQVTLVQ LDNYGPWTVT PSPRREVDLQ TLQSRLYADL SQAIGTRDGY VFFTRFDNMI
AVTNGLDLEA HARVQESIRN RYPITASLSI GTGSTPADAL VGATGALQQQ GSAQDADRRE
TLLGQPIPDA ERTDDDVQIA HFDVIDATGT YTDELDAFAS FTHIEAGYAA LMRHMHDAHD
SLSFFVGGDN IIAVCPGLSD GDYEDAIAHV QDTADVALRV GVGRGASAHD AGMGAKHALE
VAREHDTIVE RSGRQ
