ID J5PW62_SACK1 Unreviewed; 467 AA.
AC J5PW62;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=acid phosphatase {ECO:0000256|ARBA:ARBA00012646};
DE EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646};
GN Name=YBR092C {ECO:0000313|EMBL:EJT44168.1};
GN Synonyms=SKDI02G2000 {ECO:0000313|EMBL:CAI4055472.1};
GN ORFNames=SKDI_02G2000 {ECO:0000313|EMBL:CAI4055472.1}, SKUD_201103
GN {ECO:0000313|EMBL:EJT44168.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT44168.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT44168.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT44168.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT44168.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT44168.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT44168.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT44168.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4055472.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4055472.1};
RA Byrne P K.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000032};
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; OX365897; CAI4055472.1; -; Genomic_DNA.
DR EMBL; AACI03000428; EJT44168.1; -; Genomic_DNA.
DR AlphaFoldDB; J5PW62; -.
DR STRING; 226230.J5PW62; -.
DR HOGENOM; CLU_020880_3_1_1; -.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 2.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002753};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..467
FT /note="acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003785204"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 64..388
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 263..276
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 408..416
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 467 AA; 52715 MW; 975BCCF07B1E6DDB CRC64;
MFKSVVYSVL AAALVNAGTI PLGKLADVAK IGTQEDIFPF LGGAGPYFSF PGDYGISRDL
PEGCEMKQLH MLARHGERYP TYSKGATITK TWYKLSNYTR QFNGSLSFLN DDYEFFIRDN
DDLEMETTMA NSNDVLNPYT GEMDAKRHAR EFLAQYGYMF ENQTSFPIFA ASSERVHDTA
QYFIDGLGDQ FNISLQTVSE AMSAGANTLS AGNACPGWDE DANDDILDKY DTTYLGDIAK
RLNKENKGLN LTSSDANTLF AWCAYELNAR GYSDVCDIFT RDELVHYSYG QDLTSFYQDG
PGYDMIRSVG ANLFNATLKL LKQSEIQDQK VWLSFTHDTD ILNYLTTIGI IDDKNNLTAD
YVPFMDNTFH KSWYVPQGAR VYTEKFQCSN STYVRYAIND AVVPIETCST GPGFSCEVND
FYDYAEKRVA GTDFLKVCNV SSVSNVTELT FYWDWHTTHY NDTLLKQ
//
