MPTA_NATPD
ID MPTA_NATPD Reviewed; 309 AA.
AC Q3IR95;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=NP_2514A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49348.1; -; Genomic_DNA.
DR RefSeq; WP_011322974.1; NC_007426.1.
DR AlphaFoldDB; Q3IR95; -.
DR SMR; Q3IR95; -.
DR STRING; 348780.NP_2514A; -.
DR EnsemblBacteria; CAI49348; CAI49348; NP_2514A.
DR GeneID; 3701470; -.
DR KEGG; nph:NP_2514A; -.
DR eggNOG; arCOG04301; Archaea.
DR HOGENOM; CLU_062816_1_0_2; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 109805at2157; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000002698; 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..309
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000289542"
FT SITE 158
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 309 AA; 34436 MW; EC15795869273DDB CRC64;
MSQQLPDVQA SSPDVSVGLS RVGVTGVEKL VKLHRPNDRP IVLMAEFDVF VDLPSWRKGA
DMSRNMEVVD EMLEEAVSEP ALSVEDVCGD VAERLIEKHD YTTQAEVRME AEYMIREETP
ATDRPTQATA DIIASATADE DGNTREEIGC HVVGMTVCPC SQGMSESRAR DVLEGLDVDR
DTIDAFLEEV PQPGHSQRGH ATLTVETSGD PDVDLRTLID IARDSMSARI YNLAKRPDED
HMTFESHSDA KFVEDCVRSM ANGLLEEYPD LPDDTIVRME QSNDESIHQH NAHAERVAEF
GQLRREVRD