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Database: UniProt
Entry: A0A0M8MLF8_9BASI
LinkDB: A0A0M8MLF8_9BASI
Original site: A0A0M8MLF8_9BASI 
ID   A0A0M8MLF8_9BASI        Unreviewed;       453 AA.
AC   A0A0M8MLF8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:KOS13938.1};
GN   ORFNames=Malapachy_3795 {ECO:0000313|EMBL:KOS13938.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS13938.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS13938.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS13938.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS13938.1}.
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DR   EMBL; LGAV01000004; KOS13938.1; -; Genomic_DNA.
DR   RefSeq; XP_017991570.1; XM_018138254.1.
DR   AlphaFoldDB; A0A0M8MLF8; -.
DR   STRING; 77020.A0A0M8MLF8; -.
DR   GeneID; 28730130; -.
DR   VEuPathDB; FungiDB:Malapachy_3795; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000037751; Unassembled WGS sequence.
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   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751}.
SQ   SEQUENCE   453 AA;  51079 MW;  8CBEA5D561E518B7 CRC64;
     MEDESLDTIG VCSSEDRGRL SSTLGWLDPP SHLELLQVFY VLRHGERTPV RRRLTTAEPP
     LPKRWNMCHT SHKFRQAVLR QSEEDMDSVE PGLARIQRRI EYAPHGESPH VGSSGDCLLG
     ELTDRGRMSM LRIGQALRAR YVEAEHLLPS IMSDEHANQV YFRSTYVNRT MQSLDQVIVG
     LLGDKVGQEG RFTPKVLLRD PFQEDLVPNS RTCPQLAALM TKFEKAAAQF YDPKLAALDS
     IVAPMDRGFL PRLDQGPKLS GLIDTLRSAL VHGISVPPEL QEQSVQRLME DAVIAEWFGG
     YESSDLEERR KFRRMAMGPF LSSLYGQMER RVTLGDCDPL RLGLYLGHDV TLVGLLHTLD
     VFNRNWPAFS AGISFELFRD KNASTIAHRD QISDHYVRCR YGDAELHLPG CSAAGKHLPG
     HPEFCTLEAF REVVVDRLEN PQGLTLQEEC GAF
//
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