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Database: UniProt
Entry: A3LSR5_PICST
LinkDB: A3LSR5_PICST
Original site: A3LSR5_PICST 
ID   A3LSR5_PICST            Unreviewed;       362 AA.
AC   A3LSR5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=D-threo-aldose 1-dehydrogenase {ECO:0000313|EMBL:ABN66280.2};
DE            EC=1.1.1.122 {ECO:0000313|EMBL:ABN66280.2};
GN   Name=YMT1 {ECO:0000313|EMBL:ABN66280.2};
GN   ORFNames=PICST_58212 {ECO:0000313|EMBL:ABN66280.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66280.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN66280.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC       {ECO:0000256|ARBA:ARBA00007905}.
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DR   EMBL; CP000498; ABN66280.2; -; Genomic_DNA.
DR   RefSeq; XP_001384309.2; XM_001384272.1.
DR   AlphaFoldDB; A3LSR5; -.
DR   STRING; 322104.A3LSR5; -.
DR   GeneID; 4838365; -.
DR   KEGG; pic:PICST_58212; -.
DR   eggNOG; KOG1576; Eukaryota.
DR   HOGENOM; CLU_023205_7_2_1; -.
DR   InParanoid; A3LSR5; -.
DR   OMA; AVQSYAN; -.
DR   OrthoDB; 1581031at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0047834; F:D-threo-aldose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR42686:SF1; ALDO_KET_RED DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42686; GH17980P-RELATED; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:ABN66280.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   DOMAIN          32..318
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
SQ   SEQUENCE   362 AA;  41057 MW;  3419F0AB5C8888E1 CRC64;
     MPEFLEPQTN ESQAIGDSIV VQPYSIANLP PLVVGGAVFN TQYSSNPSSL PIQEILEDAF
     AKGLNAIDTS PYYGPSEILL GEALKKISFP RQEYYICTKA GRVKLDDFDY SRDSVRKSVE
     RSLERLNTSY LDLVYMHDIE FVKEDEIFDA LKELKLLKTE GLIKNFGISG YPVRFLHKIA
     SRSVGIPEIG PLDAVLSYSN GCIQNTRLFE FYDQFFDDCK LKKLSNGSIL SMSLLRSDIT
     HSFHPASKEL KDKVYDIAHL LKKEYNGLEL ADLATRFALR KWLFETVHQA DSSNLHWNPS
     TSIVLGVSNV EELDVAIRCY WQVKNNIDNI NTKDDILFEK VKNLLGPEHF NEVWPSGIDG
     RQ
//
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