MPTA_METST
ID MPTA_METST Reviewed; 313 AA.
AC Q2NI42;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Msp_0294;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(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}.
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DR EMBL; CP000102; ABC56704.1; -; Genomic_DNA.
DR RefSeq; WP_011405904.1; NC_007681.1.
DR AlphaFoldDB; Q2NI42; -.
DR SMR; Q2NI42; -.
DR STRING; 339860.Msp_0294; -.
DR EnsemblBacteria; ABC56704; ABC56704; Msp_0294.
DR GeneID; 41324867; -.
DR KEGG; mst:Msp_0294; -.
DR eggNOG; arCOG04301; Archaea.
DR HOGENOM; CLU_062816_1_0_2; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 109805at2157; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000001931; 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..313
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000289540"
FT SITE 163
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 313 AA; 35165 MW; A1FC6CC3B1338CC9 CRC64;
MTVSEFPDTQ DKQPSIPISL TRVGVTGVKK LIKIKREDKR PIILIPTFDA FVDLPSTQKG
VHMSRNPEAI SEIVDEAANQ SEIHLENICA NLVKRLLEKH EYALHAETEA RGEYIINKLS
PVSKRKTQET THIIARAIAM KDDEGNISVR KMIGAEVIGM TVCPCAQESV EKDSKDKLLE
FLDEETTQKV LDVVTFASHN QRGVGTILLE VPEKQDVNVD DLIKIIQDAM SSPVCEILKR
PDENRIVTNA HQNPVFVEDC VRNMVIGLLE KYPNLPDDSV VTIKQVNQES IHQHNAYAEK
VASFGKLREE NKE
