G3PP_PYRAB
ID G3PP_PYRAB Reviewed; 238 AA.
AC Q9V1B3; G8ZGM4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000250|UniProtKB:Q58832};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q58832};
GN OrderedLocusNames=PYRAB05140; ORFNames=PAB2019;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49436.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69903.1; -; Genomic_DNA.
DR PIR; E75169; E75169.
DR RefSeq; WP_010867638.1; NC_000868.1.
DR AlphaFoldDB; Q9V1B3; -.
DR SMR; Q9V1B3; -.
DR STRING; 272844.PAB2019; -.
DR EnsemblBacteria; CAB49436; CAB49436; PAB2019.
DR GeneID; 1495416; -.
DR KEGG; pab:PAB2019; -.
DR PATRIC; fig|272844.11.peg.549; -.
DR eggNOG; arCOG02291; Archaea.
DR HOGENOM; CLU_045011_8_3_2; -.
DR OMA; TYHNVKF; -.
DR OrthoDB; 93004at2157; -.
DR PhylomeDB; Q9V1B3; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..238
FT /note="Glyceraldehyde 3-phosphate phosphatase"
FT /id="PRO_0000107332"
SQ SEQUENCE 238 AA; 27909 MW; 06FB4CE5DA5B784A CRC64;
MIKVIFFDLD DTLVDTTKLA ELARRNAIEN MIRHGLPVDF ETAYSELMEL IKEYGSNFPH
HFDYLLRRLD LPYNPKWVSA GVIAYHNTKF AYLREVPGAR KVLIRLRELG YRLGIITDGN
PVKQWEKILR LEIDDFFEHV IISDFEGVKK PHPKIFKKAL KAFNVDAQEA LMVGDRLYSD
IYGAKNVGMK TVWFKYGKYS KEELEYREYA DYEIEKLQDL LKVIENENGS NKEVHPAR
