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Database: UniProt
Entry: A1VII2_POLNA
LinkDB: A1VII2_POLNA
Original site: A1VII2_POLNA 
ID   A1VII2_POLNA            Unreviewed;       324 AA.
AC   A1VII2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   OrderedLocusNames=Pnap_0135 {ECO:0000313|EMBL:ABM35460.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM35460.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
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DR   EMBL; CP000529; ABM35460.1; -; Genomic_DNA.
DR   RefSeq; WP_011799570.1; NC_008781.1.
DR   AlphaFoldDB; A1VII2; -.
DR   STRING; 365044.Pnap_0135; -.
DR   KEGG; pna:Pnap_0135; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_6_1_4; -.
DR   OMA; FKLWGNM; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000000644; 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; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21708:SF42; 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   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABM35460.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000644}.
FT   DOMAIN          4..104
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          197..317
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   324 AA;  34426 MW;  2286AD7090C04D15 CRC64;
     MKACIYGAGA IGGWIGSGLA RAGCSVSVLA RGATLDALQL HGLRLHDGKQ ITSQAVASSD
     TPAELGVQDL VVLAVKAPSL PEVARQIRPL LGPDTLVMTA MNGVPWWFLQ GFGGALAGRR
     LTSVDPDGML AETLPLHHII GCVVHASCSV DEPGQVQHHF GKQLIVGEPS GEQTTRAQQL
     AALLEKAGFE AVVSAQIQKD IWFKLWGNMT VNPISALTGA TIDRIMDDEL VRGFISRVML
     EAKEIGARLG ISIDQQPEDR HQITRKLGAV KTSMLQDVEA GKALELDALV AAVRELGQLT
     GVQTPYTDAL LGLARLKARV KGLY
//
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