ID A8N2P7_COPC7 Unreviewed; 410 AA.
AC A8N2P7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 18-JUN-2025, entry version 85.
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=CC1G_01861 {ECO:0000313|EMBL:EAU92816.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU92816.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU92816.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU92816.1}.
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DR EMBL; AACS02000001; EAU92816.1; -; Genomic_DNA.
DR RefSeq; XP_001829181.1; XM_001829129.2.
DR AlphaFoldDB; A8N2P7; -.
DR FunCoup; A8N2P7; 224.
DR STRING; 240176.A8N2P7; -.
DR GeneID; 6005607; -.
DR KEGG; cci:CC1G_01861; -.
DR VEuPathDB; FungiDB:CC1G_01861; -.
DR eggNOG; ENOG502QPT5; Eukaryota.
DR InParanoid; A8N2P7; -.
DR OMA; RKEPFQV; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR050838; Ketopantoate_reductase.
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: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:UP000001861}.
FT DOMAIN 3..187
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 253..401
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 410 AA; 44832 MW; 33CD629FB7143787 CRC64;
MRFHILGLGP IGSLVAHNLR RYLSPEHGIT LIFKNKEQAL TRERCLRVEN NGVVTKSSGF
DMEVFNNSPL PVRKGRAPIV TPTPPVTSPA IANLTQTPEP IQSLIISAKA HQTVPAIRLL
EPRLKPSSTI VLLQNGMGVY EELLNTVFRN PEQRPHIILA SNTHGAYFFD GQRVIHAGIG
ALEFGIAPDY RGRNFEAALE AATPANPSPP LLIKDIAVEG DPEYPHYRSL RDTVAALKGL
GALHTSWKPI SAIQLAMRRK VVVNSVINPL TALMRCRNGE IFKSEAGQSI CSSVAAEAAA
AFAAQIKAET SVFLKEMANE GVDPTTIDTG RIPPSLTQES LEKEILRVAS VTAGNQSSML
VDLERGRDTE IEYMNGYLTR LGQSYGVPMP VTSMLYNLVK MRTQIPLDQM
//
