ID G3AIH3_SPAPN Unreviewed; 464 AA.
AC G3AIH3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Secreted acid phosphatase {ECO:0000313|EMBL:EGW34443.1};
GN ORFNames=SPAPADRAFT_134430 {ECO:0000313|EMBL:EGW34443.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW34443.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; GL996500; EGW34443.1; -; Genomic_DNA.
DR RefSeq; XP_007374027.1; XM_007373965.1.
DR AlphaFoldDB; G3AIH3; -.
DR STRING; 619300.G3AIH3; -.
DR GeneID; 18869814; -.
DR KEGG; spaa:SPAPADRAFT_134430; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; G3AIH3; -.
DR OMA; TGEMDAK; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
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:UP000000709}.
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 337
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 62..386
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 214..436
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 263..276
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 406..414
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 464 AA; 51983 MW; 3A3DFFC64C98C7C3 CRC64;
MVAISKLINN GLLLAGQAVY QDLATPEQSS VQQYNIIRFL GGSAPYLQRD GFGISVDFPE
QCTIEQVQLL SRHGERYPAK SDGANFEPIY QKFVNYNGTF SGQLEFLNDY EYFVPNKNNY
EKETSPSNSQ GTFSGTSNAF RHGAAFRAKY NSLYKENSTL QVFSSNSGRC YQTSNYFARG
FLGDAYEEDE TVKYHVISED ASSGVNSLTP RNSCPNYNST ANTGLVAKYN TSSYLQPIAD
RLVKPNPGLN LTATDVSYLF SWCAYEINVR GASPFCDLFT NEEFIKNSYH TDLSDYYSIG
PGHNDSRVIG STLVNATLAL LKDNDNENKI WLSFTHDTDL EFYHSALGLV EPKDDLPVDH
IPFPNPYVHS SIVPQGARIE TEKLKCGDDY YVRFIINDSV IPIPTCADGP GFSCKLEDYE
EYIQSRIGNL DFVEQCNMNS SNPASVSFYW DYNTVTYDAP LGDF
//
