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Database: UniProt
Entry: M1N2Q1_9CLOT
LinkDB: M1N2Q1_9CLOT
Original site: M1N2Q1_9CLOT 
ID   M1N2Q1_9CLOT            Unreviewed;       309 AA.
AC   M1N2Q1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-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=Cspa_c39650 {ECO:0000313|EMBL:AGF57722.1};
OS   Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF57722.1, ECO:0000313|Proteomes:UP000011728};
RN   [1] {ECO:0000313|EMBL:AGF57722.1, ECO:0000313|Proteomes:UP000011728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL   Submitted (FEB-2013) 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   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {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; CP004121; AGF57722.1; -; Genomic_DNA.
DR   RefSeq; WP_015394035.1; NZ_AOIF01000041.1.
DR   AlphaFoldDB; M1N2Q1; -.
DR   STRING; 36745.CLSAP_37440; -.
DR   KEGG; csr:Cspa_c39650; -.
DR   PATRIC; fig|931276.5.peg.3998; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_6_0_9; -.
DR   OrthoDB; 9772736at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000011728; Chromosome.
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; 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|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW   ECO:0000313|EMBL:AGF57722.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011728}.
FT   DOMAIN          6..154
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          184..307
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   309 AA;  34702 MW;  D73BC4113A929015 CRC64;
     MDNKKVCVVG MGGVGGYVGC ILAKHFDNVY FFARGKRLES IKQNGLKLCS NAHGETVIHP
     KMASDNAEEM GAMDYIFLCV KNFSLEQVCA EILPMINENT VIIPLLNGVG ISEEARRLIG
     KGTIIDGLVY IISGSDKDFV IHHTSSYCNI HIGCEVKKNL EDSILLEVQK LLQSEEITCI
     IEKDIIAAIW EKYILNCAFN VITAYYNATI GELRKNENAI MQVKLLLNEA CKVARELKIN
     IDDNLEEIHF NRIMYKQSDQ ATSSLQRDME AGRQSELEVF SGKLLQLAAS CEIKIPTTEF
     FYEELKKKC
//
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