ID   G3PP_PYRFU              Reviewed;         240 AA.
AC   Q8U040;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000250|UniProtKB:Q58832};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q58832};
GN   OrderedLocusNames=PF1777;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81901.1; -; Genomic_DNA.
DR   RefSeq; WP_011012918.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U040; -.
DR   SMR; Q8U040; -.
DR   STRING; 186497.PF1777; -.
DR   PRIDE; Q8U040; -.
DR   EnsemblBacteria; AAL81901; AAL81901; PF1777.
DR   GeneID; 41713595; -.
DR   KEGG; pfu:PF1777; -.
DR   PATRIC; fig|186497.12.peg.1848; -.
DR   eggNOG; arCOG02291; Archaea.
DR   HOGENOM; CLU_045011_8_3_2; -.
DR   OMA; TYHNVKF; -.
DR   OrthoDB; 93004at2157; -.
DR   PhylomeDB; Q8U040; -.
DR   Proteomes; UP000001013; 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; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..240
FT                   /note="Glyceraldehyde 3-phosphate phosphatase"
FT                   /id="PRO_0000107333"
SQ   SEQUENCE   240 AA;  28077 MW;  D307F4B0358F0E70 CRC64;
     MRRIKVIFFD LDDTLVDTSK LAEVARKNAI ENMIRHGMPV DFDTAYNELL ELIKEYGSNF
     PYHFDYLLRR LDLEYNPKWV AAGVIAYHNT KFTYLREVPG ARKTLLRLKK EGYMTGIITD
     GNPIKQWEKI LRLELDDFFE HVMISDFEGV KKPHPKIFKK ALKAFNVKPE EAIMVGDRLY
     SDIYGAKNVG MKTVWFKYGK YAELDLEYKE YADYVITELP QLLEVLEREN GSDKEVHSSG