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Database: UniProt
Entry: U5S354_9CLOT
LinkDB: U5S354_9CLOT
Original site: U5S354_9CLOT 
ID   U5S354_9CLOT            Unreviewed;       309 AA.
AC   U5S354;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=CAETHG_3877 {ECO:0000313|EMBL:AGY78078.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY78078.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY78078.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY78078.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT   systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(2014).
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}.
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DR   EMBL; CP006763; AGY78078.1; -; Genomic_DNA.
DR   RefSeq; WP_013238424.1; NZ_CP012395.1.
DR   AlphaFoldDB; U5S354; -.
DR   KEGG; cah:CAETHG_3877; -.
DR   PATRIC; fig|1341692.11.peg.3897; -.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000017590; 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; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          3..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   309 AA;  33647 MW;  9028E5CFF6CC054E CRC64;
     MKIAILGAGA MGSLYATYLS CIHEVTLLDS YKPQVDAINT NGLTKVEKDN TESNYTIKAS
     ISGTDIGIQD LLIVFVKSIN TFDAVKENQA IIGPKTIVMT LQNGAGNNHD IANFVKKEHI
     IVGTSSHNSV SLGLGKFFHS GCGPTNIGPD FPCDESQKAV KIVAQAMCQC NLTVNIIDNI
     QKVLWGKLFV NCGVNALSAI MECNLGKIHS NPYLWEICTK VVHECVLVAK ADGTCFNQAE
     ALETVQHVCI SDAAGYASMY QDRQHKRRTE IDKINGVVAN LGQTYCIDTP YNEMLVDQIH
     ALEQSYLLS
//
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