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Database: UniProt
Entry: W4M6L0_9BACT
LinkDB: W4M6L0_9BACT
Original site: W4M6L0_9BACT 
ID   W4M6L0_9BACT            Unreviewed;       259 AA.
AC   W4M6L0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   18-JUN-2025, entry version 46.
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};
DE   Flags: Fragment;
GN   ORFNames=ETSY2_20680 {ECO:0000313|EMBL:ETX05830.1};
OS   Candidatus Entotheonella gemina.
OC   Bacteria; Pseudomonadati; Nitrospinota/Tectimicrobiota group;
OC   Candidatus Tectimicrobiota; Candidatus Entotheonellia;
OC   Candidatus Entotheonellales; Candidatus Entotheonellaceae;
OC   Candidatus Entotheonella.
OX   NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX05830.1, ECO:0000313|Proteomes:UP000019140};
RN   [1] {ECO:0000313|EMBL:ETX05830.1, ECO:0000313|Proteomes:UP000019140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX   PubMed=24476823; DOI=10.1038/nature12959;
RA   Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA   Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA   Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA   Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT   "An environmental bacterial taxon with a large and distinct metabolic
RT   repertoire.";
RL   Nature 506:58-62(2014).
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:ETX05830.1}.
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DR   EMBL; AZHX01000856; ETX05830.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4M6L0; -.
DR   HOGENOM; CLU_1071537_0_0_7; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000019140; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR013752; KPA_reductase.
DR   InterPro; IPR051402; KPR-Related.
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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019140}.
FT   DOMAIN          3..99
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          130..244
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETX05830.1"
SQ   SEQUENCE   259 AA;  27946 MW;  DB3E6099732F4B78 CRC64;
     VSPVQATDDP AQAGQADLIL VAVKAWQIPE VAPAIRPLLG PETVVLPLQN GLEAASQLVE
     VLGEASVLGG TCAIYSYIEA PGCIEHIGIE PTVTIGERDR MARPRTGAIR QCLEEAGIVA
     QVAPDINVPL WEKFFVLRWG IIGAVTRAPA GVLRRLPQMR EMIDQAGREV IGVARAHRVP
     LSDDMLQRNM ELLDSLPPQA TTSLQRDVMA GRPSEIDAQA GALVRLGQHV QVPTPLHAFL
     FHAILPLELQ ARGEIQFSD
//
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