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Database: UniProt
Entry: A0A395HEM7_9EURO
LinkDB: A0A395HEM7_9EURO
Original site: A0A395HEM7_9EURO 
ID   A0A395HEM7_9EURO        Unreviewed;       382 AA.
AC   A0A395HEM7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=BO80DRAFT_343997 {ECO:0000313|EMBL:RAL06421.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL06421.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL06421.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL06421.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-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; KZ824419; RAL06421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HEM7; -.
DR   STRING; 1448316.A0A395HEM7; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_343997; -.
DR   OrthoDB; 1354873at2759; -.
DR   Proteomes; UP000249402; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT   DOMAIN          111..191
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          234..366
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   382 AA;  42208 MW;  01B6C689E2D22021 CRC64;
     MQNAEEASKD SGKRRLSGRI HILGVGNVGT FVAHSLMSRP SPPPVTLLLH NPDLYSSWLA
     KKKCLALNSN GLDDIKTGFD VNVLDGRSWH SFPYWDENGE VVAETEDVED VKAPVTAMAL
     ESVKHRLTPD STVLLLQNGM GVVDEVNEKV FPDPQNRPNY MYGIISHGLA RRKEPFQVAH
     TGIGTTILGP ALSANSTGVV SENKDDWAPS TKYLLRTLTL TPPLVAVAET PSSLMLYQLE
     KLAMNAVINP LTAVMNCENG ELLYNYSFTR VMRLLLLEIS SVICALPELQ GIPGIESRFS
     PERLRWMVTQ LANKTAKNHS SMLQDVRAGK TTEIEYLNGY IVRRGEELGV KCVVNYMMKH
     LVLAKQQASK QRDASAIPID IL
//
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