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Database: UniProt
Entry: A0A0D1Z017_EXOME
LinkDB: A0A0D1Z017_EXOME
Original site: A0A0D1Z017_EXOME 
ID   A0A0D1Z017_EXOME        Unreviewed;       471 AA.
AC   A0A0D1Z017;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV10_09111 {ECO:0000313|EMBL:KIV88192.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV88192.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV88192.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV88192.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KN847526; KIV88192.1; -; Genomic_DNA.
DR   RefSeq; XP_016219766.1; XM_016374222.1.
DR   AlphaFoldDB; A0A0D1Z017; -.
DR   STRING; 212818.A0A0D1Z017; -.
DR   GeneID; 27326956; -.
DR   VEuPathDB; FungiDB:PV10_09111; -.
DR   HOGENOM; CLU_031468_10_3_1; -.
DR   OMA; INEMVVY; -.
DR   OrthoDB; 1354873at2759; -.
DR   Proteomes; UP000054302; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT   DOMAIN          47..233
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          296..428
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  52375 MW;  57A5741E657A5828 CRC64;
     MSESRSWWSG PPPVDASPSN TPTFESQPLH SDALDEIEEE KLLTRRVHVI GLGSIGTLVA
     HSLKCLPNPP PVTLMLHRPD MYEQFKKSGR IIRLINKQSD VNDEQTGYDL DVLQADGYWD
     YEADAPLGFP ANPRQLDESL PTGETFISTL VAAVKSTATV TAMRSIKHRV DSRSTICFMQ
     NGLGQIDELN REVFTDPETR PTYMLGVISH GCHMRGHFTV MHAGFGTVAL GIHRDPDRYP
     LPRQSSMPDL DQLSLEEKRM YFPTDKDLFS NLSSRYLLRT LTRSPVLACA AFPYLDLLQL
     QLEKLSANAI INPLTALLNV PNGALLHNGN LSVVHRLLLA EISLVIRSLP ELKGIPNVRN
     RFSATRLEHL LLGITARTAQ NSSSMREDAR YAQPTEIDYI NGYIVRRGEE QGIKCALNYM
     LMQLIKAKTL TQLNAATLAV PYGTVRVEAR ESSAGVVTLD DHSIPARGDV Q
//
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