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Database: UniProt
Entry: A0A3A1VEK6_9BACL
LinkDB: A0A3A1VEK6_9BACL
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ID   A0A3A1VEK6_9BACL        Unreviewed;       322 AA.
AC   A0A3A1VEK6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
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   ORFNames=D3P08_04120 {ECO:0000313|EMBL:RIX59349.1};
OS   Paenibacillus nanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=393251 {ECO:0000313|EMBL:RIX59349.1, ECO:0000313|Proteomes:UP000266482};
RN   [1] {ECO:0000313|EMBL:RIX59349.1, ECO:0000313|Proteomes:UP000266482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22867 {ECO:0000313|EMBL:RIX59349.1,
RC   ECO:0000313|Proteomes:UP000266482};
RA   Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA   Laiz L., Saiz-Jimenez C.;
RT   "Paenibacillus aracenensis nov. sp. isolated from a cave in southern
RT   Spain.";
RL   Submitted (SEP-2018) 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 + 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|ARBA:ARBA00000784,
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:RIX59349.1}.
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DR   EMBL; QXQA01000002; RIX59349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A1VEK6; -.
DR   OrthoDB; 9800163at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000266482; 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:UniProtKB-UniPathway.
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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-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   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266482}.
FT   DOMAIN          3..162
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          195..316
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   322 AA;  34857 MW;  7B20AF0767381560 CRC64;
     MGIHIVGGGA IGLLFAAKLA LAEAGATLWT RTEAQSRRIC EEGLLLVNKQ GEEQLVRVAS
     EWLNGSRLSA MEMEDEMWIL LAVKQTAIGS ELLSSLKALS DKARNGASVI CLQNGIGHLE
     KLADALGGTP VYAAVTTDGA KREDSRTVKH TGIGELWFGE WDANGQKKAE KSEIAQKMLL
     SSLQKAGFHA ILSKNMKNRI YQKLLINAVI NPLTALFDVT NGELPQHDGR LRLMRALHKE
     TYEILVAAGM ERSEDRWDAV LDVCSRTSAN VSSMLADVRA GRPTEIEAIN GAVSRLAKQL
     GRESPLNDAM TALIAPYGEA TL
//
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