ID A0A081CD61_PSEA2 Unreviewed; 484 AA.
AC A0A081CD61;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phytase {ECO:0000313|EMBL:GAK64607.1};
GN ORFNames=PAN0_006d2821 {ECO:0000313|EMBL:GAK64607.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK64607.1};
RN [1] {ECO:0000313|EMBL:GAK64607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK64607.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF830073; GAK64607.1; -; Genomic_DNA.
DR RefSeq; XP_014656950.1; XM_014801464.1.
DR AlphaFoldDB; A0A081CD61; -.
DR GeneID; 26303767; -.
DR HOGENOM; CLU_020880_0_1_1; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
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.
PE 4: Predicted;
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:UP000053758};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..484
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001755686"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 372
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 64..420
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 229..481
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 278..292
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 445..460
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 484 AA; 53189 MW; 79178ED16E420D64 CRC64;
MRQLKPAILA LASALGYGSS LWPSTQHGEP VDPNILTNFG AWSFYVPGGD VGRYDIPDKS
FPGCEVDQVN LFMRHDFRGP SKGVGSGIAT MISKLVNAST ADNADSKFSV SDGQLHPELE
FLAKLNETYS AVTPELLTSY GEQDAHSSGY HFGNRYGHLL GKKDWYNAPV NQSLPVFART
TDQSRVNVTS WAFSEGFLGL NWRERLAAPL LTLPDSSSTF NDSLAVGTCP FSAKDTSSDK
AFAAWNSVYL PKVVSRLQRA LPNLNLTTSD VQAMQNACPF QSAYLGRLSP FCAIFTLREW
ELYSYGQDLQ QYENAGYGGP LGRAWSVGWV NELLARLTET RVKDHTSTNT TLDESTTTFP
IGLPVYLDFT HDTQIASAIA VLGLLKDQIS PTSYPKKDRL WNSAHIVPMG ARIIVERLKC
ENKKSKYVRV LLNDAVVPLS GLKECNSHAQ GRLHASAGLC KVEDFVDSQS FAQAGGNWNN
CFLK
//
