MPTA_HALSA
ID MPTA_HALSA Reviewed; 311 AA.
AC Q9HNX6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=VNG_1901C;
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: 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; AE004437; AAG20094.1; -; Genomic_DNA.
DR PIR; B84341; B84341.
DR RefSeq; WP_010903394.1; NC_002607.1.
DR AlphaFoldDB; Q9HNX6; -.
DR SMR; Q9HNX6; -.
DR STRING; 64091.VNG_1901C; -.
DR PaxDb; Q9HNX6; -.
DR EnsemblBacteria; AAG20094; AAG20094; VNG_1901C.
DR GeneID; 5953154; -.
DR GeneID; 62887250; -.
DR KEGG; hal:VNG_1901C; -.
DR PATRIC; fig|64091.14.peg.1453; -.
DR HOGENOM; CLU_062816_1_0_2; -.
DR InParanoid; Q9HNX6; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 109805at2157; -.
DR PhylomeDB; Q9HNX6; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..311
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000147741"
FT SITE 158
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 311 AA; 34439 MW; F1F4109854921078 CRC64;
MSQQLPDVQA TEPDVSVGLS EVGVTGVEKL VEIAREDDRP IVLMAEFEVY VDLPRGRKGI
DMSRNMRVID ETLEDAVREP IYRVEEMCGE VAERLLEKHD YTTTATVEMN AELMLREETP
ASDLPTQGTI DIIASATAQE DAPTREEIGA RVVGMTVCPC SQQMMSETAR RKLAELGVGE
DAVREFLRDV PQAGHSQRGH ATLTVEAGGD PDVNLMDLVS VARDSMSARI YNTAKRPDED
HMTYESHANA KFVEDCVRSM ARGVVEEFDH LPEDAVVTMK QSNDESIHQH NAHAERVAEF
GQLREEVGSG E