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Database: UniProt
Entry: A0A1K0H463_9BASI
LinkDB: A0A1K0H463_9BASI
Original site: A0A1K0H463_9BASI 
ID   A0A1K0H463_9BASI        Unreviewed;       568 AA.
AC   A0A1K0H463;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   05-FEB-2025, entry version 29.
DE   SubName: Full=Related to 2-dehydropantoate 2-reductase {ECO:0000313|EMBL:SAM58951.1};
GN   ORFNames=UBRO2_01961 {ECO:0000313|EMBL:SYW77769.1}, UBRO_01137
GN   {ECO:0000313|EMBL:SAM58951.1};
OS   Ustilago bromivora.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=307758 {ECO:0000313|EMBL:SAM58951.1, ECO:0000313|Proteomes:UP000179920};
RN   [1] {ECO:0000313|EMBL:SAM58951.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UB2112 {ECO:0000313|EMBL:SAM58951.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000179920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UB2112 {ECO:0000313|Proteomes:UP000179920};
RA   Guldener U., Guldener U.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SYW77769.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UB2 {ECO:0000313|EMBL:SYW77769.1};
RA   Guldener U.;
RL   Submitted (AUG-2018) 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; LT558117; SAM58951.1; -; Genomic_DNA.
DR   EMBL; ULHB01000028; SYW77769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K0H463; -.
DR   OrthoDB; 5160at5257; -.
DR   Proteomes; UP000179920; Chromosome i.
DR   Proteomes; UP000658997; 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:UP000658997}.
FT   DOMAIN          198..289
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          393..554
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          136..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  62291 MW;  63279805074FE86D CRC64;
     MRYHVLGVGS IGSLIAFHLK RSVKLQRQLL QPRPSFSKSK RELLLSNLSN KRPPQNQGTI
     VSSLSLPPYV QTELPDPQQT SVTLHLRRKA FGKQAKQRFV NSIVVEQDGV RDIEGGFQTD
     FNSSPTDVIA SIVRRNWSNQ PEGEEEESED RFLISRTTTS SSPEAAAIRD QTSSKTPLPD
     HDGGISLIST LEGLHSQPRA SPIDSLIITT KCDATLSALE GIRDRIHPWS TIVLLQNGMG
     VLDTLFDTFF KDPDQRPNFV LASTTHGCWR KGPLDVVHAS TGTLHFGIVP SGRAGQDGIE
     KSRVPYGQTI ARVRGVVLPS RGEAAKKAAR GWERFSPDTD SNAIEEIPDL GSPSKLLSIA
     SIPDKPSLRT LRATVAALLS LPLNVEWEPI REFQLRSLRK LVINACINPL TALADCKNGD
     LFGNPVAKDA MWSVCLEAGM VLEAQVREHL ASGATASPRQ RASASLSAED LILRSDETGE
     PILHPSLTPQ ALFQEVQRVA RMTAANWSSM HSDLKNRRGS TEIDHINGYI SALGRGYNID
     TTANDLLTNL VKLKTTRVTG TGRLRREQ
//
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