ID A0A011QNS2_ACCRE Unreviewed; 295 AA.
AC A0A011QNS2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 18-JUN-2025, entry version 42.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN Name=panE {ECO:0000313|EMBL:EXI90942.1};
GN ORFNames=AW11_00283 {ECO:0000313|EMBL:EXI90942.1};
OS Accumulibacter regalis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Candidatus Accumulibacter.
OX NCBI_TaxID=522306 {ECO:0000313|EMBL:EXI90942.1, ECO:0000313|Proteomes:UP000022141};
RN [1] {ECO:0000313|EMBL:EXI90942.1, ECO:0000313|Proteomes:UP000022141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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 + 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 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|ARBA:ARBA00004994, 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:EXI90942.1}.
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DR EMBL; JEMY01000003; EXI90942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QNS2; -.
DR STRING; 1454004.AW11_00283; -.
DR PATRIC; fig|1454004.3.peg.290; -.
DR eggNOG; COG1893; Bacteria.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000022141; 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:0050661; F:NADP binding; IEA:TreeGrafter.
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 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; IPR003710; ApbA.
DR InterPro; IPR050838; Ketopantoate_reductase.
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; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000022141}.
FT DOMAIN 3..147
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 170..293
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 295 AA; 30907 MW; 411686E4DD984F1E CRC64;
MKVAVMGAGA VGCYYGGMLA RAGHAVVLIG RPQHVAAVCR DGLFMHTQSF QAQVPMQAST
DAGAVRGAQL VLCCVKSPDT ETAAMAMAPH LDPDACLLSL QNGVDNAERW QAVLRREVAP
AVVYVATEMA GPGFVKHHGR GELVIGPSSC SDELLALFAA AAIPVTISDN VAGALWAKLI
VNCVYNAVSA ITQLPYGHLV QGDGVPGVMR DVMAECLAVA QAAGVVVAGD MWQAVQQIAH
TMPGQLSSTA QDLARHKPSE IDHLNGYVLR KGEALAVPTP VNRVLYALVK LLESR
//
