ID A0A0D6XQS1_9STAP Unreviewed; 311 AA.
AC A0A0D6XQS1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 Name=panE_1 {ECO:0000313|EMBL:SUM58502.1};
GN ORFNames=NCTC13832_02252 {ECO:0000313|EMBL:SUM58502.1}, TP70_05475
GN {ECO:0000313|EMBL:KIX90927.1};
OS Staphylococcus microti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=569857 {ECO:0000313|EMBL:KIX90927.1, ECO:0000313|Proteomes:UP000032366};
RN [1] {ECO:0000313|EMBL:KIX90927.1, ECO:0000313|Proteomes:UP000032366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22147 {ECO:0000313|EMBL:KIX90927.1,
RC ECO:0000313|Proteomes:UP000032366};
RA Guo J.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUM58502.1, ECO:0000313|Proteomes:UP000254100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13832 {ECO:0000313|EMBL:SUM58502.1,
RC ECO:0000313|Proteomes:UP000254100};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; JXWY01000033; KIX90927.1; -; Genomic_DNA.
DR EMBL; UHDT01000001; SUM58502.1; -; Genomic_DNA.
DR RefSeq; WP_044360165.1; NZ_UHDT01000001.1.
DR AlphaFoldDB; A0A0D6XQS1; -.
DR STRING; 569857.TP70_05475; -.
DR PATRIC; fig|569857.6.peg.1407; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000032366; Unassembled WGS sequence.
DR Proteomes; UP000254100; Unassembled WGS sequence.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) 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:SUM58502.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT DOMAIN 4..154
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..306
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 311 AA; 34586 MW; EA208F299DD49086 CRC64;
MTKIAIAGAG AMGSRIGSYI KRAGYDVTLI DAWPDHVRAI NDKGLEVQTE TDTYIVEIPA
VLPEDVTGTF DLIVILTKSM QSEAMIHQLK DKGAIHQDTA ILTMMNGLGH DERFAKIVPH
EQVFLAVTMW TAGMRGPGQI LLEGQGSIEL QRADGQADER TETINKIFND AGLNAKISDN
VFQSIWSKAT LNSVLNPLCS ILNKTIYEFG SYEHARAMVT PIIDEIVAVA KARNVELDGA
ALLEKIEAAY PKETQGLHYP SMHQDLYNRR YTEVDYLNGQ ISKYGREANI PTPNNDMLTH
LIHQLEMKYI K
//
