ID   G3PP_PYRHO              Reviewed;         241 AA.
AC   O59346;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000250|UniProtKB:Q58832};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q58832};
GN   OrderedLocusNames=PH1655;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of the probable haloacid dehalogenase protein (PH1655)
RT   from Pyrococcus horikoshii OT3.";
RL   Submitted (JUL-2007) to the PDB data bank.
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; BA000001; BAA30767.1; -; Genomic_DNA.
DR   PIR; G71045; G71045.
DR   RefSeq; WP_010885722.1; NC_000961.1.
DR   PDB; 2HOQ; X-ray; 1.70 A; A=1-241.
DR   PDBsum; 2HOQ; -.
DR   AlphaFoldDB; O59346; -.
DR   SMR; O59346; -.
DR   STRING; 70601.3258084; -.
DR   EnsemblBacteria; BAA30767; BAA30767; BAA30767.
DR   GeneID; 1442503; -.
DR   KEGG; pho:PH1655; -.
DR   eggNOG; arCOG02291; Archaea.
DR   OMA; TYHNVKF; -.
DR   OrthoDB; 93004at2157; -.
DR   EvolutionaryTrace; O59346; -.
DR   Proteomes; UP000000752; 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   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..241
FT                   /note="Glyceraldehyde 3-phosphate phosphatase"
FT                   /id="PRO_0000107334"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           16..33
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           40..54
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           61..68
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           75..92
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           99..109
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           121..130
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           143..146
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           153..163
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   STRAND          170..175
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           181..186
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           205..209
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   STRAND          211..216
FT                   /evidence="ECO:0007829|PDB:2HOQ"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:2HOQ"
SQ   SEQUENCE   241 AA;  28259 MW;  6EAF5A3F82254B0E CRC64;
     MVKVIFFDLD DTLVDTSKLA EIARKNAIEN MIRHGLPVDF ETAYSELIEL IKEYGSNFPY
     HFDYLLRRLD LPYNPKWISA GVIAYHNTKF AYLREVPGAR KVLIRLKELG YELGIITDGN
     PVKQWEKILR LELDDFFEHV IISDFEGVKK PHPKIFKKAL KAFNVKPEEA LMVGDRLYSD
     IYGAKRVGMK TVWFRYGKHS ERELEYRKYA DYEIDNLESL LEVLARESSS NKKVHPPRQQ
     I