ID B6YVY2_THEON Unreviewed; 242 AA.
AC B6YVY2;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019531};
GN OrderedLocusNames=TON_0817 {ECO:0000313|EMBL:ACJ16305.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16305.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ16305.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16305.1,
RC ECO:0000313|Proteomes:UP000002727};
RX PubMed=18790866; DOI=10.1128/JB.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.J., Lee J.H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- FUNCTION: Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-
CC phosphate in vitro. {ECO:0000256|ARBA:ARBA00003513}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00007958}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000855; ACJ16305.1; -; Genomic_DNA.
DR RefSeq; WP_012571777.1; NC_011529.1.
DR AlphaFoldDB; B6YVY2; -.
DR STRING; 523850.TON_0817; -.
DR GeneID; 7017120; -.
DR KEGG; ton:TON_0817; -.
DR PATRIC; fig|523850.10.peg.824; -.
DR eggNOG; arCOG02291; Archaea.
DR HOGENOM; CLU_045011_8_3_2; -.
DR OrthoDB; 27736at2157; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd04305; HAD_Neu5Ac-Pase_like; 1.
DR Gene3D; 1.10.150.520; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR02253; CTE7; 1.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR46470; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR PANTHER; PTHR46470:SF2; N-ACYLNEURAMINATE-9-PHOSPHATASE; 1.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ACJ16305.1}.
SQ SEQUENCE 242 AA; 28135 MW; 02BF5C51E5EFB905 CRC64;
MIRVVFFDLD DTLVDTSKLA EMARKNAIEN MVRHGLPVDF ETAYHELLEL INEYGSNFGR
HFDYLLRRLD LPNNPKWIAA GVIAYHNTKF AYLKSVKGAR KVLLELKKDG FGLGVITDGD
PIKQWEKILR LELDEYFDEV FISNDLGVKK PHRKIFEKAL RKFNVEPHEA LMVGDRLYSD
IYGAKQVGMR TVWFKYGKYA NRELDYLEYA DFAIKSLGEV LEIVRGLNLE EKERADKEVH
AD
//
