ID L2FUN0_COLFN Unreviewed; 325 AA.
AC L2FUN0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=CGGC5_9668 {ECO:0000313|EMBL:ELA30047.1}, CGGC5_v004500
GN {ECO:0000313|EMBL:KAF4488217.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA30047.1};
RN [1] {ECO:0000313|EMBL:ELA30047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA30047.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF4488217.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4488217.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4488217.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4488217.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P., Shirasu K.;
RT "Genome sequencing and assembly of multiple isolates from the
RT Colletotrichum gloeosporioides species complex.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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; KB020821; ELA30047.1; -; Genomic_DNA.
DR EMBL; ANPB02000002; KAF4488217.1; -; Genomic_DNA.
DR RefSeq; XP_007280920.1; XM_007280858.1.
DR AlphaFoldDB; L2FUN0; -.
DR STRING; 1213859.L2FUN0; -.
DR EnsemblFungi; ELA30047; ELA30047; CGGC5_9668.
DR HOGENOM; CLU_031468_2_0_1; -.
DR InParanoid; L2FUN0; -.
DR OrthoDB; 5478361at2759; -.
DR Proteomes; UP000011096; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF40; REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14497)-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 Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000011096};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..160
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 191..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 325 AA; 35797 MW; 1E8A7A9F7D576E6B CRC64;
MATEKQTEVL LYGLGAIGSF YAFILSRVPA VRLTVVARSN YDAVKANGII LKSENHGEHI
IRPYKVVKTA AEADAKFDYI VCAHKAITQD AVPAQIAPAV DEKRSTIVII QNGVGNEVPF
RSAFPHATII SCVTWTGASQ PQPGNIIHTK SEDMQIGLYS NDADQSVEKQ RLDEFAAFLT
EGKTVFQVVP NIQVQRWEKV VWNAAWNSLT TLTLLDTHSW LSSSDGATPL TRRLMTEVID
VAKGCNVPID YDLIDKLINK ILAMHPIGSS MQADYKAGRP MEVDIILGYP YRKGKELGIS
TPTLDTIYII LTGTNLRLLR ENGQA
//
