ID   G3PP_METKA              Reviewed;         233 AA.
AC   Q8TWR2;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000250|UniProtKB:Q58832};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q58832};
GN   OrderedLocusNames=MK0970;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM02183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009439; AAM02183.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8TWR2; -.
DR   SMR; Q8TWR2; -.
DR   STRING; 190192.MK0970; -.
DR   PRIDE; Q8TWR2; -.
DR   EnsemblBacteria; AAM02183; AAM02183; MK0970.
DR   KEGG; mka:MK0970; -.
DR   HOGENOM; CLU_045011_8_3_2; -.
DR   OMA; TYHNVKF; -.
DR   Proteomes; UP000001826; 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; 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; TIGR01509; HAD-SF-IA-v3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Glyceraldehyde 3-phosphate phosphatase"
FT                   /id="PRO_0000107330"
SQ   SEQUENCE   233 AA;  26692 MW;  D73940D03DA38818 CRC64;
     MIKAVLFDVD DTLYPSSKLA EEARRNAIRA MIEAGLETDL SEEELYRELQ EVVKEYGSNH
     PRHFDLLLRR IGADPEPKLV AAAVVAYHDT KFAYLKPYPD VIPTLMQLRE MGFKLGAVTS
     GLAVKQWEKL IRLGIHHFFH EVVISEEIGV EKPNPKIFIE AARRLGVKPE EAVYVGDRLD
     KDIRGANRAG MVTVRIRRGK YQDMEPRNDD DVPDFEIDRP RELLDVVREL AKD