PHO2_YARLI
ID PHO2_YARLI Reviewed; 358 AA.
AC P30887; Q6CAE8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acid phosphatase;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PHO2; OrderedLocusNames=YALI0D03465g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=1423722; DOI=10.1007/bf00352435;
RA Treton B.Y., le Dall M.-T., Gaillardin C.;
RT "Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a
RT genomic sequence from the yeast Yarrowia lipolytica identifies a new
RT phosphatase.";
RL Curr. Genet. 22:345-355(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 -!- FUNCTION: Probably serves to scavenge phosphorus for growing cells.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. {ECO:0000305}.
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DR EMBL; X65225; CAA46331.1; -; Genomic_DNA.
DR EMBL; CR382130; CAG80552.1; -; Genomic_DNA.
DR PIR; S19993; S19993.
DR RefSeq; XP_502364.1; XM_502364.1.
DR AlphaFoldDB; P30887; -.
DR SMR; P30887; -.
DR STRING; 4952.CAG80552; -.
DR EnsemblFungi; CAG80552; CAG80552; YALI0_D03465g.
DR GeneID; 2910307; -.
DR KEGG; yli:YALI0D03465g; -.
DR VEuPathDB; FungiDB:YALI0_D03465g; -.
DR HOGENOM; CLU_045192_0_0_1; -.
DR InParanoid; P30887; -.
DR OMA; MGNDDGF; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; IEA:InterPro.
DR Gene3D; 3.40.1210.10; -; 1.
DR InterPro; IPR030048; SurE.
DR InterPro; IPR002828; SurE-like_Pase/nucleotidase.
DR InterPro; IPR036523; SurE-like_sf.
DR PANTHER; PTHR30457; PTHR30457; 1.
DR Pfam; PF01975; SurE; 1.
DR SUPFAM; SSF64167; SSF64167; 1.
DR TIGRFAMs; TIGR00087; surE; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..358
FT /note="Acid phosphatase"
FT /id="PRO_0000033476"
FT REGION 21..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /evidence="ECO:0000255"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 228
FT /note="G -> V (in Ref. 1; CAA46331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38003 MW; 0362F01F892E693B CRC64;
MKFSTIALPL LASAALAQTN SSHSGTNATS HNSTVPNENS KTTIVVTNDD SWASANIRAF
YDELKKEGYN VFMFAPALQQ SGTGGTFVLP KNTTLAKGAE WGSAPVGAPA WGQDEKDDHI
WYFDGTPGAA VTFGFDYALP KFHNNITVDL VVSGPNEGWN LGPFVYTLSG TEGAMYTSVL
RGVPAIAFSG ENKHTYYANA SNSETASHNI YAKASTAIVK NLLKNAKGRP SVLPYGVGLS
VNLPLVGDID PTGKCTDPKP IFTRQTGRGA ITDKLVFNET TGLFKYGDIK SDATKACLNG
DCFLPDETDV INNWGCYSSI SVVSTDYDAP GALAAEAQFL NRGLVEFAPT GYGSFPGN
