ID   MPTA_METHJ              Reviewed;         328 AA.
AC   Q2FNB7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   18-JUN-2025, entry version 91.
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};
GN   OrderedLocusNames=Mhun_2334;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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         formate + diphosphate + 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000254; ABD42038.1; -; Genomic_DNA.
DR   RefSeq; WP_011449296.1; NC_007796.1.
DR   AlphaFoldDB; Q2FNB7; -.
DR   SMR; Q2FNB7; -.
DR   FunCoup; Q2FNB7; 1.
DR   STRING; 323259.Mhun_2334; -.
DR   EnsemblBacteria; ABD42038; ABD42038; Mhun_2334.
DR   GeneID; 3923052; -.
DR   KEGG; mhu:Mhun_2334; -.
DR   eggNOG; arCOG04301; Archaea.
DR   HOGENOM; CLU_062816_1_0_2; -.
DR   InParanoid; Q2FNB7; -.
DR   OrthoDB; 53087at2157; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:InterPro.
DR   GO; GO:0044682; F:GTP cyclohydrolase IV activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:2001118; P:tetrahydromethanopterin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.270.10; Urate Oxidase; 1.
DR   HAMAP; MF_01527_A; GTP_cyclohydrol_A; 1.
DR   InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR   InterPro; IPR022840; GTP_cyclohydrolase_MptA.
DR   NCBIfam; TIGR00294; GTP cyclohydrolase MptA; 1.
DR   PANTHER; PTHR36445; GTP CYCLOHYDROLASE MPTA; 1.
DR   PANTHER; PTHR36445:SF1; GTP CYCLOHYDROLASE MPTA; 1.
DR   Pfam; PF02649; GCHY-1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Reference proteome.
FT   CHAIN           1..328
FT                   /note="GTP cyclohydrolase MptA"
FT                   /id="PRO_0000289541"
FT   SITE            171
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   328 AA;  36818 MW;  5338252B90362DE9 CRC64;
     MSLLKTSERG FSRELPDVQS TLPDVRINLT RVGVKNVKKL VEVTRPGKRP VIFISNFDIF
     VDLPGSLKGA NLSRNFEVID EVLQSAIEGE VKEIEQLCSR VARRLLDKHE YADRTEVQMR
     SEFMVAGETP VTGTLCQEVV KVFASAIAQR TFKDPIVRKS IGAEVTGMTA CPCAQNIMQE
     RAREVMENLD IAKDKIESFF KEVPMATHNQ RGRGFLSIET DDESHVKLEK IIMILKQSMS
     TPIFELLKRG DEGHVVLSAH KNPRFVEDCV REMARRVHAE FGDLPGDSVV TIAQDNEESI
     HQHDAFAERQ ATIAELADEI NGENLDVS
//