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Database: UniProt
Entry: V6U1B4_GIAIN
LinkDB: V6U1B4_GIAIN
Original site: V6U1B4_GIAIN 
ID   V6U1B4_GIAIN            Unreviewed;       100 AA.
AC   V6U1B4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN   ORFNames=GSB_7871 {ECO:0000313|EMBL:ESU44983.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU44983.1, ECO:0000313|Proteomes:UP000018040};
RN   [1] {ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA   Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA   Nash T.;
RT   "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT   Pig).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESU44983.1, ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS {ECO:0000313|EMBL:ESU44983.1,
RC   ECO:0000313|Proteomes:UP000018040};
RX   PubMed=24307482; DOI=10.1093/gbe/evt197;
RA   Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA   Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA   Nash T.E.;
RT   "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT   Pig).";
RL   Genome Biol. Evol. 5:2498-2511(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESU44983.1}.
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DR   EMBL; AHHH01000012; ESU44983.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6U1B4; -.
DR   EnsemblProtists; ESU44983; ESU44983; GSB_7871.
DR   VEuPathDB; GiardiaDB:DHA2_7871; -.
DR   VEuPathDB; GiardiaDB:GL50581_1470; -.
DR   VEuPathDB; GiardiaDB:GL50803_007871; -.
DR   VEuPathDB; GiardiaDB:QR46_3220; -.
DR   Proteomes; UP000018040; 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; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT   DOMAIN          14..100
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   100 AA;  10974 MW;  372C0B2CE4CC4566 CRC64;
     MQGSTPHSSE DVVTLLYRVT GKVQGVFFRK YTKKEADALS LVGHVMNNED GSVSGIVQGP
     KSHVDAFVKY LHKGSPKSIV KRVDIQASAR VEASAFEIRR
//
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