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Database: UniProt
Entry: A0A1H9J5S5_9RHOB
LinkDB: A0A1H9J5S5_9RHOB
Original site: A0A1H9J5S5_9RHOB 
ID   A0A1H9J5S5_9RHOB        Unreviewed;       337 AA.
AC   A0A1H9J5S5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN04488092_11421 {ECO:0000313|EMBL:SEQ82117.1};
OS   Thalassovita taeanensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=657014 {ECO:0000313|EMBL:SEQ82117.1, ECO:0000313|Proteomes:UP000198634};
RN   [1] {ECO:0000313|EMBL:SEQ82117.1, ECO:0000313|Proteomes:UP000198634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22007 {ECO:0000313|EMBL:SEQ82117.1,
RC   ECO:0000313|Proteomes:UP000198634};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOEP01000014; SEQ82117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9J5S5; -.
DR   STRING; 657014.SAMN04488092_11421; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000198634; Unassembled WGS sequence.
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   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198634}.
FT   DOMAIN          3..102
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          190..298
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   337 AA;  34985 MW;  7E97617A84C1DBD4 CRC64;
     MNIAIIGAGN IGTAMAALIG SAGGDVTVVA RGHRLDTIRR DGVSLDDRGT LHAAQVTAVT
     ALDQVHDAVF LCVKAQDLGA AVAANAAGIG PETLVVPMIN GLPFWYFYGA GGTVPFSDPA
     GQLAYHLRPE QVLGAVLLMT VQMTAAGRAV STNTPTLSLA PVVAGADSAA ISRLIDLLCA
     SGVRTDLSAD IRQQVLVKLM SNIATNPLSA LTGENLAQIG RELSLRSIAY QLADEVRAWA
     DRMLGRSLPP NAWLGDLLLD AGDFPTSMLQ DARAGRVLEL DAICRAPLAL AGEGAMPCLA
     ALVAQLDSAD TFPLTGAPRS TAVERLLFLT SLERNSE
//
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