G3PP_METJA
ID G3PP_METJA Reviewed; 228 AA.
AC Q58832;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000303|PubMed:25848029};
DE EC=3.1.3.- {ECO:0000305|PubMed:25848029};
GN OrderedLocusNames=MJ1437;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC -!- FUNCTION: Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-
CC phosphate in vitro. {ECO:0000269|PubMed:25848029}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99446.1; -; Genomic_DNA.
DR PIR; D64479; D64479.
DR RefSeq; WP_010870955.1; NC_000909.1.
DR AlphaFoldDB; Q58832; -.
DR SMR; Q58832; -.
DR STRING; 243232.MJ_1437; -.
DR DNASU; 1452341; -.
DR EnsemblBacteria; AAB99446; AAB99446; MJ_1437.
DR GeneID; 1452341; -.
DR KEGG; mja:MJ_1437; -.
DR eggNOG; arCOG02291; Archaea.
DR HOGENOM; CLU_045011_8_3_2; -.
DR InParanoid; Q58832; -.
DR OMA; TYHNVKF; -.
DR OrthoDB; 93004at2157; -.
DR PhylomeDB; Q58832; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050124; F:N-acylneuraminate-9-phosphatase activity; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0046380; P:N-acetylneuraminate biosynthetic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..228
FT /note="Glyceraldehyde 3-phosphate phosphatase"
FT /id="PRO_0000107329"
SQ SEQUENCE 228 AA; 26064 MW; C832F9F435ABC3FF CRC64;
MIKGILFDLD DTLYNSSEFV EIARREAVKS MIDAGLNIDF EEAMNILNKI IKDKGSNYGK
HFDDLVKAVL GKYDPKIITT GIITYHNVKV ALLRPYPHTI KTLMELKAMG LKLGVITDGL
TIKQWEKLIR LGIHPFFDDV ITSEEFGLGK PHLEFFKYGL KRMGLKAEET VYVGDRVDKD
IKPAKELGMI TVRILKGKYK DMEDDEYSDY TINSLQELVD IVKNLKKD