ID F0XMR9_GROCL Unreviewed; 347 AA.
AC F0XMR9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 13-SEP-2023, entry version 47.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=CMQ_6381 {ECO:0000313|EMBL:EFX01439.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX01439.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.169; Evidence={ECO:0000256|RuleBase:RU362068};
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; GL629794; EFX01439.1; -; Genomic_DNA.
DR RefSeq; XP_014170921.1; XM_014315446.1.
DR AlphaFoldDB; F0XMR9; -.
DR STRING; 655863.F0XMR9; -.
DR GeneID; 25979808; -.
DR eggNOG; ENOG502QWBM; Eukaryota.
DR HOGENOM; CLU_031468_2_1_1; -.
DR InParanoid; F0XMR9; -.
DR OrthoDB; 1816688at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
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: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 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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 9..167
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 205..327
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 347 AA; 37202 MW; CE0330461902DCD2 CRC64;
MAISSKANVL LVGSGGVGTM GAYALESGGL AEVTAVLRSN FSTVSEKGFD ISSIDHGEVK
AWKPKKIVSQ VPDVSDEGVV PFDFVVVSTK NVADVSPTVV DIIAPAVTAG HTAIVLLQNG
LNIEVPVIAA FPQNVVISGV SRIGAAETSH GVIVHNDRDR LHIGPFDNAN LPAELQTATA
QRFATMYGAS GKVVVEFGAT AQEVAWTRWR KLIYNACYNS IAAVTLLDSG RLRLARSPVV
ELLRPAMLEI VAIAKAQGHV LPLELVEEII EAEPIEIYFK PSMQQDVEKG NYTEFENIVG
EPLRTARKLG VPAPTLTVLY GILRAMQWRT KEQKGLITLE SARAQLA
//