MPTA2_METAR
ID MPTA2_METAR Reviewed; 309 AA.
AC Q0W8U7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=GTP cyclohydrolase MptA 2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE EC=3.5.4.39 {ECO:0000255|HAMAP-Rule:MF_01527};
DE AltName: Full=GTP cyclohydrolase IV 2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN Name=mptA2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN OrderedLocusNames=UNCMA_29770; ORFNames=LRC194;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ35196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM114193; CAJ35196.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q0W8U7; -.
DR SMR; Q0W8U7; -.
DR STRING; 351160.LRC194; -.
DR PRIDE; Q0W8U7; -.
DR EnsemblBacteria; CAJ35196; CAJ35196; LRC194.
DR KEGG; rci:LRC194; -.
DR PATRIC; fig|351160.9.peg.3062; -.
DR eggNOG; arCOG04301; Archaea.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000663; 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 2"
FT /id="PRO_0000289544"
FT SITE 158
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 309 AA; 34896 MW; 9A561A5131220B4E CRC64;
MILPDVQATK SEVAINLSRV GVTNVKKLVK VARPDKRPII LISTFNMYVD LPSERRGANL
SRNFEVIDEV LEDMVKSPVY EIEDLCGEVA RRLLNRHEYA TRSEVHMDSE LIVKRKTPQT
EMQSQKVVKV FAKAIAERGE AIKVRRVIGS EVIGITACPC AQEIMRVSAE NELQNLGVPQ
EKIDAFLNKI PMATHNQRGR GIVSIETAGE YEVPLNTLIN IIEQSMSTMS FELLKRGDEY
EVVRNAHANP KFVEDCVRDM ARRVVTEFKD LPDDAVVKIK QINEESIHQH NAFAELSTTM
GKLRTEIGQ