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Database: UniProt
Entry: A0A0G2HLM5_9PEZI
LinkDB: A0A0G2HLM5_9PEZI
Original site: A0A0G2HLM5_9PEZI 
ID   A0A0G2HLM5_9PEZI        Unreviewed;       331 AA.
AC   A0A0G2HLM5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=UCDDA912_g04156 {ECO:0000313|EMBL:KKY35883.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY35883.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY35883.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY35883.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY35883.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY35883.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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}.
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:KKY35883.1}.
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DR   EMBL; LCUC01000144; KKY35883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HLM5; -.
DR   STRING; 1214573.A0A0G2HLM5; -.
DR   OrthoDB; 5478361at2759; -.
DR   Proteomes; UP000034680; 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:UP000034680}.
FT   DOMAIN          5..163
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          193..320
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   331 AA;  35743 MW;  B53BBF48190F6574 CRC64;
     MAPKVLIFGA GSIGGVYSYI LSRAVPAANI TVTCRSNYEA VSKNGFTVNS TLWGKGLNVR
     PSVARDVTEA TQASEGDPYD YVIVTSKALN TTPTTAELIK PAVASGTTTI VLIQNGIDTE
     WTFAKLFPEN PILSTVVYLP ATQVEPGVIE HQEVELLHIG TYPASAPQPH KDAAKAFSDL
     LTLAKASSKV HDDVQAQRWS KLIVNASWNS ICALTRCRDR PLLDVRNQSG GFKDFIRGVM
     LEIAATAQAY GYAEINEELV DVQLRRASVR QLPGIQPSMM ADALAGRNME VDAIVGNTVR
     LAREKGVPTP MLQTIYFLAS GLDTSFTLSR S
//
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