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Database: UniProt
Entry: A0A4R5QL94_9PROT
LinkDB: A0A4R5QL94_9PROT
Original site: A0A4R5QL94_9PROT 
ID   A0A4R5QL94_9PROT        Unreviewed;       325 AA.
AC   A0A4R5QL94;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 18.
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   ORFNames=E2C06_02805 {ECO:0000313|EMBL:TDH64284.1};
OS   Dankookia rubra.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Roseomonadaceae; Dankookia.
OX   NCBI_TaxID=1442381 {ECO:0000313|EMBL:TDH64284.1, ECO:0000313|Proteomes:UP000295096};
RN   [1] {ECO:0000313|EMBL:TDH64284.1, ECO:0000313|Proteomes:UP000295096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM30602 {ECO:0000313|EMBL:TDH64284.1,
RC   ECO:0000313|Proteomes:UP000295096};
RX   PubMed=27225458; DOI=10.1007/s12275-016-6054-3;
RA   Kim W.H., Kim D.H., Kang K., Ahn T.Y.;
RT   "Dankookia rubra gen. nov., sp. nov., an alphaproteobacterium isolated from
RT   sediment of a shallow stream.";
RL   J. Microbiol. 54:420-425(2016).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:ARBA00048793};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDH64284.1}.
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DR   EMBL; SMSJ01000002; TDH64284.1; -; Genomic_DNA.
DR   RefSeq; WP_133287049.1; NZ_SMSJ01000002.1.
DR   AlphaFoldDB; A0A4R5QL94; -.
DR   OrthoDB; 247668at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000295096; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR   FunFam; 3.40.50.720:FF:000307; 2-dehydropantoate 2-reductase; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR051402; KPR-Related.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF005089; PRK06522.1-4; 1.
DR   PANTHER; PTHR21708:SF45; 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|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295096}.
FT   DOMAIN          3..171
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          198..317
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   325 AA;  34305 MW;  4F63252FBC1BA61C CRC64;
     MKICVFGAGA IGGLMAARLA AKGETEVTVI ARGPHLAAMQ ANGLKLISDG QETVVRPRCV
     ASAAEAGRQD YVVITLKAPA LAGAAAQMQP LIGEGTTIVS AVNGVPWWYF YKLAGPYEGR
     RVESVDPTGE VGRLLPPEKV LGCIIYPAAE VSEPGVIEHT YGDRFTLGEP DGSRSDRAMA
     LSAALSAAGF KAPVRPKIRD EIWVKLWGNL AFNPLSALTT ATLDVITGDA ELRAVCRQMM
     LEAQAVAESL GVRFAIDVDK RIAGAAEVGA HKTSMLQDLE RGRPMEVDAL LGSVVELAGI
     TEVPAPTCRT VLALLRTRAR LAGCY
//
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