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Database: UniProt
Entry: A0A5C8PHY6_9HYPH
LinkDB: A0A5C8PHY6_9HYPH
Original site: A0A5C8PHY6_9HYPH 
ID   A0A5C8PHY6_9HYPH        Unreviewed;       315 AA.
AC   A0A5C8PHY6;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 20.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN   Name=panE {ECO:0000313|EMBL:TXL73428.1};
GN   ORFNames=FHP25_21075 {ECO:0000313|EMBL:TXL73428.1};
OS   Vineibacter terrae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Vineibacter.
OX   NCBI_TaxID=2586908 {ECO:0000313|EMBL:TXL73428.1, ECO:0000313|Proteomes:UP000321638};
RN   [1] {ECO:0000313|EMBL:TXL73428.1, ECO:0000313|Proteomes:UP000321638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-CFT640 {ECO:0000313|EMBL:TXL73428.1,
RC   ECO:0000313|Proteomes:UP000321638};
RA   Lin S.-Y., Tsai C.-F., Young C.-C.;
RT   "New taxonomy in bacterial strain CC-CFT640, isolated from vineyard.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC       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|ARBA:ARBA00048793,
CC         ECO:0000256|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994, 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:TXL73428.1}.
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DR   EMBL; VDUZ01000025; TXL73428.1; -; Genomic_DNA.
DR   RefSeq; WP_147848950.1; NZ_VDUZ01000025.1.
DR   AlphaFoldDB; A0A5C8PHY6; -.
DR   OrthoDB; 247668at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000321638; 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:UniProtKB-UniPathway.
DR   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR   FunFam; 3.40.50.720:FF:000307; 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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   NCBIfam; NF005094; PRK06522.2-5; 1.
DR   PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321638}.
FT   DOMAIN          6..149
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          179..303
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   315 AA;  32914 MW;  7BABAC947E4635A4 CRC64;
     MKLLSLGAGA LGGYFGGRLH QAGTDVTFLV RAARAEKLKA EGLRIQSPRG DAALTVKTVG
     DGALGGPYDI VLLSCKAYDL DSAMDAIAPA VGVDTVVVPV LNGIRHLDAL DVRFGRERVV
     GGVARIGATL SPDGAVVHSS PFAAISTGER DKGRAPRPVL VELAEALKRA GVDGGLHPDI
     MQDMWDKWVM LGTLASLTCA FRAPVGDILA TKDGEAIVRE TIAECSQVAA AAGHAPSEAA
     LKMVEGIMLT RGSMFAASLL HDVERGGRVE ADHIVGDLLA RAAAAGIATP NLRFAYAHLQ
     AYERRRARER AGEAL
//
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