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Database: UniProt
Entry: V5EZP7_KALBG
LinkDB: V5EZP7_KALBG
Original site: V5EZP7_KALBG 
ID   V5EZP7_KALBG            Unreviewed;       358 AA.
AC   V5EZP7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:EST09413.1};
GN   ORFNames=PSEUBRA_SCAF11g01203 {ECO:0000313|EMBL:EST09413.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09413.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KI545853; EST09413.1; -; Genomic_DNA.
DR   RefSeq; XP_016294402.1; XM_016434297.1.
DR   AlphaFoldDB; V5EZP7; -.
DR   STRING; 1365824.V5EZP7; -.
DR   GeneID; 27416896; -.
DR   eggNOG; ENOG502QT3Y; Eukaryota.
DR   HOGENOM; CLU_031468_2_0_1; -.
DR   OMA; WDYVVVT; -.
DR   OrthoDB; 1548520at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; 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; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR21708:SF42; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377}.
FT   DOMAIN          7..166
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          217..343
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   358 AA;  39428 MW;  EC8A2594730B8A98 CRC64;
     MSKPVHILIV GAGAVGCFYA SKLHQTHSER QILVSLVCRS NYAAIAANGV SLQTHSFGDY
     HFTPHKVFSS IPEAGEAGID WDYVVVTTKA LPDVTNDAHD IRPVVKRGVE GSCIVLIQNG
     VGIEEVHRVA YGENPIVSAV TVISAEQIKH GVIKQNRWTR ITMGTYTNGQ AKPNSLLSDS
     ALLSKLTSTT DTHIKNLVAW FSATGIKDAE FSPELSLQQT RWHKLCINAS MNPSSVLSGG
     TTNSRMALDP ELRTHLRACM DEIFLTAPKI LGIEFDEKKH ASPERILKST ERNTSGKPSM
     LLDWQAGRPM ELEVILGNPL RIARRDGWEM PRLQTLYALL KMAQVRKRED AEGAKAKL
//
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