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
//