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Database: UniProt
Entry: A0A017SEP5_ASPRC
LinkDB: A0A017SEP5_ASPRC
Original site: A0A017SEP5_ASPRC 
ID   A0A017SEP5_ASPRC        Unreviewed;       368 AA.
AC   A0A017SEP5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   02-APR-2025, entry version 31.
DE   SubName: Full=Putative 2-dehydropantoate 2-reductase {ECO:0000313|EMBL:EYE94715.1};
GN   ORFNames=EURHEDRAFT_457382 {ECO:0000313|EMBL:EYE94715.1};
OS   Aspergillus ruber (strain CBS 135680).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1388766 {ECO:0000313|EMBL:EYE94715.1, ECO:0000313|Proteomes:UP000019804};
RN   [1] {ECO:0000313|Proteomes:UP000019804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 135680 {ECO:0000313|Proteomes:UP000019804};
RX   PubMed=24811710; DOI=10.1038/ncomms4745;
RA   Kis-Papo T., Weig A.R., Riley R., Persoh D., Salamov A., Sun H., Lipzen A.,
RA   Wasser S.P., Rambold G., Grigoriev I.V., Nevo E.;
RT   "Genomic adaptations of the halophilic Dead Sea filamentous fungus Eurotium
RT   rubrum.";
RL   Nat. Commun. 5:3745-3745(2014).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KK088425; EYE94715.1; -; Genomic_DNA.
DR   RefSeq; XP_040638403.1; XM_040784426.1.
DR   AlphaFoldDB; A0A017SEP5; -.
DR   STRING; 1388766.A0A017SEP5; -.
DR   GeneID; 63699550; -.
DR   HOGENOM; CLU_031468_2_1_1; -.
DR   OrthoDB; 3609at2759; -.
DR   Proteomes; UP000019804; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR051402; KPR-Related.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR21708:SF30; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019804}.
FT   DOMAIN          8..163
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          213..340
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   368 AA;  40767 MW;  BD29ADDAD05F7883 CRC64;
     MSQSKLRILL IGGGGIGIVT AYALETGGLA EVTAILRSNY AVVEKNGFTI DSVDHGYIQG
     WRPSHTRNTI PNKEEKIFDY LILTTKNIPD IPPALPDIIA PAVTPSHTSI ILIQNGVNIE
     HPFRERFPTN PIISGVSFTS ATEVKPGFIR HDDYDRVRLG PFPHPRNQDP SDSELSAKAT
     TATQTFITAY NPNANINTNN CTIDVQFDID VPATCWRKLI YNASFNPISA ILRMDITRMR
     VYEHVIDELV KPAMREVVAV AGALGIRVVS RGEDEEGVIG QAIRCDPPEA FFRPSMCQDV
     EKGNYMEIEN IVGEPLREGE KLGVPTPTLR TIYAILKGLQ MKVKEQRGFV EPKFNEKSQY
     AGKSESMA
//
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