ID   G3PP_METTH              Reviewed;         226 AA.
AC   O26311;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000250|UniProtKB:Q58832};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q58832};
GN   OrderedLocusNames=MTH_209;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-
CC       phosphate in vitro. {ECO:0000250|UniProtKB:Q58832}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q58832};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB84715.1; -; Genomic_DNA.
DR   PIR; F69125; F69125.
DR   RefSeq; WP_010875848.1; NC_000916.1.
DR   AlphaFoldDB; O26311; -.
DR   SMR; O26311; -.
DR   STRING; 187420.MTH_209; -.
DR   EnsemblBacteria; AAB84715; AAB84715; MTH_209.
DR   GeneID; 1470170; -.
DR   KEGG; mth:MTH_209; -.
DR   PATRIC; fig|187420.15.peg.178; -.
DR   HOGENOM; CLU_045011_8_3_2; -.
DR   OMA; TYHNVKF; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR011950; HAD-SF_hydro_IA_CTE7.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02253; CTE7; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Glyceraldehyde 3-phosphate phosphatase"
FT                   /id="PRO_0000107331"
SQ   SEQUENCE   226 AA;  25463 MW;  09ADB1225B253012 CRC64;
     MLKAVFFDID DTLYDTSGFA KLARKAALNV MIDAGLPLTQ EEAYKLLREI ISEKGSNYDR
     HFNVLTKTVF GEEKPLLIAL GMITYHNVKF ALLRPFPNTT STLIDLKSKG YRLGVISNGI
     TIKQWEKLIR LGIHHFFDEV VTSDEVGFEK PNIRIFEEAL RRMGCKPERS VMVGNKFNED
     ILGATNAGMS AILVNSELTE AERDHVEKNG LDVTVIDDIS QLKEIL