ID M2LS78_BAUPA Unreviewed; 319 AA.
AC M2LS78;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=BAUCODRAFT_575211 {ECO:0000313|EMBL:EMC97327.1};
OS Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS (Baudoinia compniacensis (strain UAMH 10762)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC97327.1, ECO:0000313|Proteomes:UP000011761};
RN [1] {ECO:0000313|EMBL:EMC97327.1, ECO:0000313|Proteomes:UP000011761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC97327.1,
RC ECO:0000313|Proteomes:UP000011761};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB445554; EMC97327.1; -; Genomic_DNA.
DR RefSeq; XP_007675761.1; XM_007677571.1.
DR AlphaFoldDB; M2LS78; -.
DR STRING; 717646.M2LS78; -.
DR GeneID; 19115706; -.
DR KEGG; bcom:BAUCODRAFT_575211; -.
DR eggNOG; ENOG502S3CY; Eukaryota.
DR HOGENOM; CLU_031468_2_0_1; -.
DR OMA; MLQDYEA; -.
DR OrthoDB; 5478361at2759; -.
DR Proteomes; UP000011761; 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:UP000011761}.
FT DOMAIN 5..142
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..302
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 319 AA; 34829 MW; 3D268D2D4D0D33DE CRC64;
MTRALIFGTG GVGCVYAYIL HKAAGVTVTT VCRTNYNAVK ENGILIRSKI FGTQRFRPKA
VQSVHEARRH GPFDYVVVCS KAFPGTAETI EPANGIGVED GYAELYPTNT LISGVVYLPV
TQCEPGVVEH GPLERFEIGT FPAASCAKPE AQEQTRMFSA MFYAGGASCP VFDDVQPRKW
IKVAVNAAWN PVTALTLCDD ANYLRSSPRA ETLIRNIMHE VGLIAAAAGY PNVITDEVIN
DDLQRPLSRL ETGGKEPSML TDVRHGRAME VEAILGNALR IGEEHGVKTP CLEVIYTLAK
ARNYAQAPDE HWKPIARHD
//
