MPTA_METBU
ID MPTA_METBU Reviewed; 317 AA.
AC Q12ZQ0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Mbur_0054;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE51076.1; -; Genomic_DNA.
DR RefSeq; WP_011498240.1; NC_007955.1.
DR AlphaFoldDB; Q12ZQ0; -.
DR SMR; Q12ZQ0; -.
DR STRING; 259564.Mbur_0054; -.
DR EnsemblBacteria; ABE51076; ABE51076; Mbur_0054.
DR GeneID; 3996851; -.
DR KEGG; mbu:Mbur_0054; -.
DR HOGENOM; CLU_062816_1_0_2; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 109805at2157; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000001979; 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; Reference proteome.
FT CHAIN 1..317
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000289535"
FT SITE 165
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 317 AA; 35543 MW; 01725F795A2C9B70 CRC64;
MELPIAQFPD VQANRPKIPI NLTRVGVTGV KKLVEIKRKD KRPIVLISTF EIFVDLPSDR
KGANLSRNFE AMDEVLEKAI NLPVYEIEKL CNDVAKSLLR RHEYATRSEV RMKSEYVVKR
EAPSTKMKCQ EVVDIFAEAT ATRLEDGDID VKKLIGAEVV GMTACPCAQE IMRDNAKTAL
RELGVGLETV MNFLNKVPMA THNQRGRGII SLEVSGDVDV SLETIIRIIE SSMSSSIVEL
LKRADEALVV ERAHQNPKFV EDCVRTMAQN IVSEFAHVPD SALVTIKQIN EESIHRHNAF
AERVALLGDL RDEIKNN