ID M2W8V2_GALSU Unreviewed; 125 AA.
AC M2W8V2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=Gasu_07030 {ECO:0000313|EMBL:EME32296.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME32296.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|RuleBase:RU004168}.
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DR EMBL; KB454487; EME32296.1; -; Genomic_DNA.
DR RefSeq; XP_005708816.1; XM_005708759.1.
DR AlphaFoldDB; M2W8V2; -.
DR STRING; 130081.M2W8V2; -.
DR EnsemblPlants; EME32296; EME32296; Gasu_07030.
DR GeneID; 17090886; -.
DR Gramene; EME32296; EME32296; Gasu_07030.
DR KEGG; gsl:Gasu_07030; -.
DR eggNOG; KOG3360; Eukaryota.
DR OMA; VCYRASA; -.
DR OrthoDB; 126107at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR10029; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR10029:SF3; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520,
KW ECO:0000313|EMBL:EME32296.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT DOMAIN 35..123
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 68
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 125 AA; 13560 MW; 868E9C40D23A37E2 CRC64;
MAGFILSSGL GSGSCGRLVL ATGATVMCRS KPIAAVALKI FGRVQGVCYR ASAAEKAEEL
NLVGWVRNNR DGTVEAEAQG TCDNLKLFVE WCKQGPDIAK VTKVEEQWKD IDTLDYSSFR
VERTV
//
