MPTA_THEVO
ID MPTA_THEVO Reviewed; 284 AA.
AC Q979C3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=GTP cyclohydrolase MptA {ECO:0000255|HAMAP-Rule:MF_01527};
DE EC=3.5.4.39 {ECO:0000255|HAMAP-Rule:MF_01527};
DE AltName: Full=GTP cyclohydrolase IV {ECO:0000255|HAMAP-Rule:MF_01527};
GN Name=mptA {ECO:0000255|HAMAP-Rule:MF_01527}; OrderedLocusNames=TV1238;
GN ORFNames=TVG1279013;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic
CC phosphate, the first intermediate in the biosynthesis of coenzyme
CC methanopterin. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate +
CC diphosphate + formate + H(+); Xref=Rhea:RHEA:25860,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58854; EC=3.5.4.39;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- SUBUNIT: Homodimer. {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; BA000011; BAB60380.1; -; Genomic_DNA.
DR RefSeq; WP_010917472.1; NC_002689.2.
DR AlphaFoldDB; Q979C3; -.
DR SMR; Q979C3; -.
DR STRING; 273116.14325476; -.
DR EnsemblBacteria; BAB60380; BAB60380; BAB60380.
DR GeneID; 1441354; -.
DR KEGG; tvo:TVG1279013; -.
DR eggNOG; arCOG04301; Archaea.
DR HOGENOM; CLU_062816_1_0_2; -.
DR OMA; ECQEVYD; -.
DR OrthoDB; 109805at2157; -.
DR PhylomeDB; Q979C3; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01527_A; GTP_cyclohydrol_A; 1.
DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR InterPro; IPR022840; GTP_cyclohydrolase_MptA.
DR PANTHER; PTHR36445; PTHR36445; 1.
DR Pfam; PF02649; GCHY-1; 1.
DR TIGRFAMs; TIGR00294; TIGR00294; 1.
PE 3: Inferred from homology;
KW Hydrolase; Iron; Metal-binding.
FT CHAIN 1..284
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000147754"
FT SITE 142
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 284 AA; 31808 MW; ED1F698243BD96BC CRC64;
MIDFLDVQAS TPDIRISVDK VGIRRMKFPI KIGDEVAILS ADLYIDIPQT RKGADMSRAV
ESIQSVLSRP SINLESLGIE ICKEALGRFN YASRVEVKIN GEYYKKSNGG YDEISLYIRT
KCGIDGNIEN LTGLSYEAIT ACPCAMETTR ALISKDIPDS ENVLYYIPTV THNQRNRTKL
IVSNNAGKIS FWDIYKVLES VQGKPLESLL KRIDEGKLVY EAHKKPKFVE DVVREVAFAA
VTLLPLSDDD MVIVSSDSEE SIHPHNAYAS MKKRALDLKK ELNL
