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Database: UniProt
Entry: A0A8H3FRQ6_9LECA
LinkDB: A0A8H3FRQ6_9LECA
Original site: A0A8H3FRQ6_9LECA 
ID   A0A8H3FRQ6_9LECA        Unreviewed;       467 AA.
AC   A0A8H3FRQ6;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   05-FEB-2025, entry version 12.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HETSPECPRED_007772 {ECO:0000313|EMBL:CAF9931016.1};
OS   Heterodermia speciosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Lecanoromycetidae; Caliciales; Physciaceae; Heterodermia.
OX   NCBI_TaxID=116794 {ECO:0000313|EMBL:CAF9931016.1, ECO:0000313|Proteomes:UP000664521};
RN   [1] {ECO:0000313|EMBL:CAF9931016.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tagirdzhanova G.;
RL   Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:CAF9931016.1}.
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DR   EMBL; CAJPDS010000057; CAF9931016.1; -; Genomic_DNA.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000664521; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 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:UP000664521}.
FT   DOMAIN          183..274
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          310..443
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..20
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  52031 MW;  903D48837A751A2B CRC64;
     MGTSLKMGTH VRTRTKKPSP QKRIHVFGVD AIGLLVAHSL AGIPNRPPIT FLTGSRSGFH
     RSEESERRIE VVTDGISDAR SGFDIEYDHP YIETEPLYSS VGSSDPQIFD RVDTAERFRL
     ADELNAVRAT SAPELVLPVE RSPVGEQTGA ADTALDASRD VMRNEAVLPD FEQGKGYSSS
     SSDDQDFISN LIVSVPAIHL RCLRKIAHRL NKESVLLFLQ NGMGFIDKVN EQVFPDPQTR
     PTYIVGVVSH IAARTKAYTV VHSGRGAIAL GVMPRGEPGP IHSLSTSARY LLRTITRTPV
     LAAVAYDQMN ILQYRLERLA IDCVIHPLTA VIECRNGELL ANFHIARMMK LILAEISLVA
     RSLPELQNVP NLQNRFDPGR LEFYVVSVAR RTSQDESQML QDIRAGRDTH IGFLNGYFIR
     KGEELGIRCV MNYMLKQMVQ AKQRSVSNRD FERLPMESQD SLVLAGR
//
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