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Database: UniProt
Entry: A0A1I1EIJ7_9BURK
LinkDB: A0A1I1EIJ7_9BURK
Original site: A0A1I1EIJ7_9BURK 
ID   A0A1I1EIJ7_9BURK        Unreviewed;       324 AA.
AC   A0A1I1EIJ7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=SAMN05216344_104207 {ECO:0000313|EMBL:SFB86496.1};
OS   Polaromonas sp. OV174.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1855300 {ECO:0000313|EMBL:SFB86496.1, ECO:0000313|Proteomes:UP000218980};
RN   [1] {ECO:0000313|EMBL:SFB86496.1, ECO:0000313|Proteomes:UP000218980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV174 {ECO:0000313|EMBL:SFB86496.1,
RC   ECO:0000313|Proteomes:UP000218980};
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; FOKZ01000004; SFB86496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1EIJ7; -.
DR   STRING; 1855300.SAMN05216344_104207; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000218980; 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:UP000218980}.
FT   DOMAIN          3..104
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          197..315
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   324 AA;  34019 MW;  D70042070EC6E372 CRC64;
     MKVCIYGAGA IGGWIGSGLA RAGCSVSVVA RGATLDALQL HGLRLIQDGR MSSQAVASSA
     APAELGVQDL VVLTVKAPSL PDVVQQIAPL LGPDTIVLTA MNGVPWWFLQ GFGGTLAGTR
     LNSVDPTGAL AQAIPAQQVI GCVVHASCSL DEPGLVRHNF GNKLILGEPS GEKSERVQRL
     AALLEKAGFE APLSEQIQQD IWFKLWGNMT MNPISALTGA TTDRILGDEL VRGFVSSIML
     EAKAIGARLG IHIEQQPEDR HAVTLKLGAF KTSMLQDVEA GKAVELDALV AAVKELGQLT
     QVATPFTDAL LGLARLQARV HGLY
//
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