ID Q9UXZ7_PYRAB Unreviewed; 216 AA.
AC Q9UXZ7;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019531};
GN OrderedLocusNames=PAB1224 {ECO:0000313|EMBL:CAB50615.1};
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844 {ECO:0000313|EMBL:CAB50615.1, ECO:0000313|Proteomes:UP000000810};
RN [1] {ECO:0000313|EMBL:CAB50615.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50615.1};
RA Genoscope;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAB50615.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50615.1};
RX PubMed=10736225; DOI=10.1006/jmbi.2000.3593;
RA Gaspin C., Cavaille J., Erauso G.;
RT "Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs:
RT lessons from the Pyrococcus genomes.";
RL J. Mol. Biol. 297:895-906(2000).
RN [3] {ECO:0000313|EMBL:CAB50615.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Orsay {ECO:0000313|EMBL:CAB50615.1};
RX PubMed=11381026; DOI=10.1101/gr.GR1653R;
RA Lecompte O., Ripp R., Puzos-Barbe V., Duprat S., Heilig R., Dietrich J.,
RA Thierry J.C., Poch O.;
RT "Genome evolution at the genus level: comparison of three complete genomes
RT of hyperthermophilic archaea.";
RL Genome Res. 11:981-993(2001).
RN [4] {ECO:0000313|EMBL:CAB50615.1, ECO:0000313|Proteomes:UP000000810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay {ECO:0000313|Proteomes:UP000000810}, and Orsay
RC {ECO:0000313|EMBL:CAB50615.1};
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G., Barbe V., Flament D., Galperin M., Heilig R., Ripp R.,
RA Lecompte O., Prieur D., Poch O., Quellerou J., Thierry J.C.,
RA Van der Oost J., 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 [5] {ECO:0000313|EMBL:CCE71182.1, ECO:0000313|Proteomes:UP000009139}
RP GENOME REANNOTATION.
RC STRAIN=GE5 {ECO:0000313|EMBL:CCE71182.1}, and GE5 / Orsay
RC {ECO:0000313|Proteomes:UP000009139};
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: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}.
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DR EMBL; AJ248288; CAB50615.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71182.1; -; Genomic_DNA.
DR PIR; A75022; A75022.
DR RefSeq; WP_010868828.1; NC_000868.1.
DR AlphaFoldDB; Q9UXZ7; -.
DR STRING; 272844.PAB1224; -.
DR GeneID; 1496011; -.
DR KEGG; pab:PAB1224; -.
DR PATRIC; fig|272844.11.peg.1827; -.
DR eggNOG; arCOG02291; Archaea.
DR HOGENOM; CLU_045011_8_3_2; -.
DR OrthoDB; 31229at2157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 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; 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; PF00702; Hydrolase; 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:CAB50615.1}.
SQ SEQUENCE 216 AA; 25007 MW; 954F55EFEAC9C815 CRC64;
MVRAILFDLD ETLISERPLV LFILPQVYEI LAKRLNVSKS EAREIFLGEI ERMRGRYEWH
DWNYFFRRFS LPFKFEELIL SYPEKITVLP GVRDTLEILR EKYRLAIVTS GPRYQILKLK
VSGLLDYFDA VITRDDVKAI KPNPKIFIAA LERLKVEPNK AVMVGDSLEQ DVLGAKALGI
KTVWINQKGD NGYNLPDFEI SSISELLEVL EDEGDI
//
