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Database: UniProt
Entry: A0A0D6ZDY3_9BACI
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ID   A0A0D6ZDY3_9BACI        Unreviewed;       307 AA.
AC   A0A0D6ZDY3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   ORFNames=UB32_02340 {ECO:0000313|EMBL:KIY23500.1};
OS   Mesobacillus subterraneus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY23500.1, ECO:0000313|Proteomes:UP000032512};
RN   [1] {ECO:0000313|EMBL:KIY23500.1, ECO:0000313|Proteomes:UP000032512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MITOT1 {ECO:0000313|EMBL:KIY23500.1,
RC   ECO:0000313|Proteomes:UP000032512};
RA   Peet K.C., Thompson J.R.;
RT   "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT   subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {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|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:KIY23500.1}.
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DR   EMBL; JXIQ01000016; KIY23500.1; -; Genomic_DNA.
DR   RefSeq; WP_044390874.1; NZ_JXIQ01000016.1.
DR   AlphaFoldDB; A0A0D6ZDY3; -.
DR   PATRIC; fig|285983.3.peg.2090; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000032512; 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; 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; PTHR21708:SF26; 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|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW   ECO:0000313|EMBL:KIY23500.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032512}.
FT   DOMAIN          3..152
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          179..299
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   307 AA;  33762 MW;  606C5A5C6D19C2B1 CRC64;
     MKILIVGAGA IGGYFGGRLL EMEANVTFLV REKRQKQLKE HGLVVTSIHG DLHVSDPQTI
     VSGSHPEPYD VILVSTKSYH LDGAIESIRP YVGDKTMILP LLNGIAHLDA LSEAFGSKKV
     IGGLCFIETT LDENGKVIQT SPVQDLIFGE RNGERSERIL QLQATFEGTK ANFRLSEKIE
     QEMWQKYLFI TPLSGITSLF RSPIGPIRDQ AQGADTLKRL LHETVEIMTA IGAPLSEGAM
     DATWNRLNDI GDGMKSSLQR DMEKSLPTEG DHLFGFLLKK AADLQIAAPT LSAVYANVDI
     YDKMLHS
//
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