ID A0A2V1AMG4_9ASCO Unreviewed; 316 AA.
AC A0A2V1AMG4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 02-APR-2025, entry version 21.
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=CXQ85_001193 {ECO:0000313|EMBL:PVH18902.1};
OS Candidozyma haemuli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Metschnikowiaceae; Candidozyma.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH18902.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH18902.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH18902.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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 + NADPH + H(+);
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:PVH18902.1}.
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DR EMBL; PKFO01000001; PVH18902.1; -; Genomic_DNA.
DR RefSeq; XP_025339842.1; XM_025484911.1.
DR AlphaFoldDB; A0A2V1AMG4; -.
DR STRING; 45357.A0A2V1AMG4; -.
DR EnsemblFungi; CXQ85_001193-t46_1; CXQ85_001193-t46_1-p1; CXQ85_001193.
DR GeneID; 37006524; -.
DR VEuPathDB; FungiDB:CXQ85_001193; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF30; 2-DEHYDROPANTOATE 2-REDUCTASE-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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000244309}.
FT DOMAIN 4..140
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 173..293
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 316 AA; 34818 MW; C90B9453DFBEB253 CRC64;
MAAYALSLNA ETTAIVRSDY EQVSKHGFQI DSVDYGTIES FKPQHVAPSI GEAAKQGPFD
FIVVTTKNIP DVSKVEELIE PLIGADSTIV LVQNGIDIGT PFVEKYPKNI VLSGVSMISS
TNYGGKISHV GHDELMVGAF FNSNLPLDQQ EMAAKTFVKL YKNDKNDCLY DENVKYTRWR
KLVYNATLNT VCTLTGVDVG RLELFGGMDL VRKAMREVLA VAKSDGVELP ESIMEFMIRS
DDGNYYEPSM LVDIRKGNYI ELEVILGNAV RIAQRNGVEA PTLALVYELL AVVQNKTKEA
KGDLDVPQER PLGGNI
//
