GenomeNet

Database: UniProt
Entry: D2PPM0_KRIFD
LinkDB: D2PPM0_KRIFD
Original site: D2PPM0_KRIFD 
ID   D2PPM0_KRIFD            Unreviewed;       331 AA.
AC   D2PPM0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   OrderedLocusNames=Kfla_1888 {ECO:0000313|EMBL:ADB30982.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Kribbellaceae; Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB30982.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADB30982.1, ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RX   PubMed=21304701;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA   Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA   Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.-P., Brettin T.;
RT   "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL   Stand. Genomic Sci. 2:186-193(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001736; ADB30982.1; -; Genomic_DNA.
DR   RefSeq; WP_012919538.1; NC_013729.1.
DR   AlphaFoldDB; D2PPM0; -.
DR   STRING; 479435.Kfla_1888; -.
DR   KEGG; kfl:Kfla_1888; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_11; -.
DR   OMA; VVRWGQR; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000007967; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT   DOMAIN          3..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          173..312
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   331 AA;  35801 MW;  90C97F2BEC558A82 CRC64;
     MTIAVYGAGG IGCYVGGRLV AGGADVVLVG RQRVADEVAE HGLHLTDYRG ADLRVTDVRF
     ETIPAAAAEA DLVLVTVKSA ATDTAAAELA EVLEPGTVVV SFQNGIRNGD LLRERLPEQL
     VLTGMVPFNV LTKGGGAFHQ GTEGGLDVQQ HAAIAPYVEV FERAGLPLTQ HADILPVQWA
     KLLLNLNNPV NALSDLPLRD QLSQRAYRRC LAAAQTETLE LLALQGIKPA QLMALPPHRI
     PTVLRLPDLL FRRVAAKMLA IDPHARSSLW EDLQAGRRTE IDYLNGEVVR LAESLGRAAP
     VNSRLVALIR QAQAGPRRAW TGEQLYRELR P
//
DBGET integrated database retrieval system