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Database: UniProt
Entry: Q0CKP4_ASPTN
LinkDB: Q0CKP4_ASPTN
Original site: Q0CKP4_ASPTN 
ID   Q0CKP4_ASPTN            Unreviewed;       540 AA.
AC   Q0CKP4;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATEG_05740 {ECO:0000313|EMBL:EAU33501.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU33501.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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; CH476601; EAU33501.1; -; Genomic_DNA.
DR   RefSeq; XP_001214918.1; XM_001214918.1.
DR   AlphaFoldDB; Q0CKP4; -.
DR   STRING; 341663.Q0CKP4; -.
DR   EnsemblFungi; EAU33501; EAU33501; ATEG_05740.
DR   GeneID; 4321315; -.
DR   VEuPathDB; FungiDB:ATEG_05740; -.
DR   eggNOG; KOG3043; Eukaryota.
DR   HOGENOM; CLU_504293_0_0_1; -.
DR   OMA; FANELVW; -.
DR   OrthoDB; 5478361at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR002925; Dienelactn_hydro.
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:SF30; 2-REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00740)-RELATED; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT   DOMAIN          19..180
FT                   /note="Dienelactone hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01738"
FT   DOMAIN          209..356
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          397..525
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   540 AA;  58709 MW;  222641AC8C3EDBC4 CRC64;
     MAIQTLQGAD ILATRLNAVV LVPDFFHGAA AQHDWIPPDS EEKQRLITDL IENQASIPKN
     VEVLREAVAA YRTVFPSVQK WAALGLCWGG KVAVLASGAE TPFAVTGQVH PGRMEQADAE
     NLTIPHIVLA SKDEPADIVN HYTDILARNG IGGHVETYTT MWHGWMGARA RLDEKESSAE
     YIRGYTQIAD FFENNNPRNT STNMAPSVLL FGVGSVGGVY LYQLQQAGCT VTAVCRSNYD
     AVQQHGFTLQ SKQFGTVTYR PDHLVRTLSD CPPDAVYDYL IVTTKSFPAS SNSRSPLAEQ
     LQPALANRPN TTIVLAQNGI EIEPEIAAAF PANPLLSAVI YLPATQIAPG VIEYPETLNV
     LELGTYPADA PAAHKASAQV LAERMRAGGS DVSVLEDVQT ARWAKLIVNA SWNPVCALAL
     CTDGDFLRCA DPFARDLVWG IMMEIVALAK AAGVPGVDEE AAAKRMAVAT RRAETRTGRE
     PSMLQDVRQG RPFEVGAIMG NAVRLERKWG VAMPRLETVY PLAKGRYEAM VRELRMSSRA
//
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