PPA5_KLULA
ID PPA5_KLULA Reviewed; 469 AA.
AC P52289; Q6CWZ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Repressible acid phosphatase;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PHO5; OrderedLocusNames=KLLA0B00286g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RA Ferminan E.;
RL Thesis (1995), University of Salamanca, Spain.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Repressed by inorganic phosphate. {ECO:0000250}.
CC -!- PTM: Glycosylated during secretion across the membrane.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; Z33995; CAA83964.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH01935.1; -; Genomic_DNA.
DR RefSeq; XP_451542.1; XM_451542.1.
DR AlphaFoldDB; P52289; -.
DR SMR; P52289; -.
DR STRING; 28985.XP_451542.1; -.
DR EnsemblFungi; CAH01935; CAH01935; KLLA0_B00286g.
DR GeneID; 2896996; -.
DR KEGG; kla:KLLA0_B00286g; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; P52289; -.
DR OMA; TGEMDAK; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 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 Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..469
FT /note="Repressible acid phosphatase"
FT /id="PRO_0000023955"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="S -> G (in Ref. 1; CAA83964)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> N (in Ref. 1; CAA83964)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="P -> S (in Ref. 1; CAA83964)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..108
FT /note="GPM -> DPL (in Ref. 1; CAA83964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52505 MW; C6169701E485691A CRC64;
MLSILLSLLS LSGTHAAPIS KDNGTVCYAL NSSTTDESIF PLLNGQGPHY DYPQSFGIPV
EVPDQCTVEH VQMLARHGER YPTASKGKLM IALWDKLKEF QGQYNGPMEV FNDYEFFVSN
TKYFDQLTNS TDVDPSNPYA GAKTAQHLGK YIAYNYGDLF SDSNPVFTSS SGRVHQTAKY
VVSSLEEELD IQLDLQIIQE NETSGANSLT PADSCMTYNG DLGDEYFENA TLPYLTDIKN
RWMKKNSNLN LTLEHDDIEL LVDWCAFETN VKGSSAVCDL FERNDLVAYS YYANVNNFYR
RGAGNPMSNP IGSVLVNASY NLLTQADELD NKVWLSFSHD TDIQQFISAL GLIDNGVTEY
SLDQVDFQNI QQLSWVTPMG GRIFTEKLKC GNASYVRYII NDVIIPVPGC TSGPGFSCPI
EDFDDYITNR LNGIDYVSSC EVQQVSNTTE LTFYWDYNEV EYNGPVSNK
