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Database: UniProt
Entry: A9WJS5_CHLAA
LinkDB: A9WJS5_CHLAA
Original site: A9WJS5_CHLAA 
ID   A9WJS5_CHLAA            Unreviewed;       320 AA.
AC   A9WJS5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
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   OrderedLocusNames=Caur_3356 {ECO:0000313|EMBL:ABY36541.1};
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36541.1, ECO:0000313|Proteomes:UP000002008};
RN   [1] {ECO:0000313|Proteomes:UP000002008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC   {ECO:0000313|Proteomes:UP000002008};
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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; CP000909; ABY36541.1; -; Genomic_DNA.
DR   RefSeq; WP_012259194.1; NC_010175.1.
DR   RefSeq; YP_001636930.1; NC_010175.1.
DR   AlphaFoldDB; A9WJS5; -.
DR   STRING; 324602.Caur_3356; -.
DR   EnsemblBacteria; ABY36541; ABY36541; Caur_3356.
DR   KEGG; cau:Caur_3356; -.
DR   PATRIC; fig|324602.8.peg.3777; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_6_1_0; -.
DR   InParanoid; A9WJS5; -.
DR   OMA; VTWVGAR; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:ABY36541.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002008}.
FT   DOMAIN          9..159
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..306
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   320 AA;  34063 MW;  8C80777F36D3A196 CRC64;
     MSVENPMRIA IVGVGGVGGY FGGRLAQAGH DVFFIARGDH LAAMRSHGLR VQSIAGDFWL
     PDVKATDQPA EVGPVDLVIV GVKGWQVREA AYAMQPLIGP ETAVLPLLNG VDAPTELAEV
     LGAEHVLAGL CRIIAYRAAP GVIVHAGVNP PSIDFGELDN RHTPRLARIQ AALEGAGIRA
     FIPENIHVAL WQKFMLICAW SGFGAATRAP IGVWRSLPET RPLVERCLQE VVDVAAARGV
     MLPDNAVSTM MAFIDSMPYE GTASLQRDIM SGQPSELASQ NGALVRLARA AGVPVPVNEM
     LYAILLPQEL AARGQLPTQR
//
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