ID A0A443YV99_9SPHI Unreviewed; 307 AA.
AC A0A443YV99;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
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 ORFNames=DPV69_12310 {ECO:0000313|EMBL:RWU07755.1};
OS Pedobacter chitinilyticus.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2233776 {ECO:0000313|EMBL:RWU07755.1, ECO:0000313|Proteomes:UP000284120};
RN [1] {ECO:0000313|EMBL:RWU07755.1, ECO:0000313|Proteomes:UP000284120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM134L-2 {ECO:0000313|EMBL:RWU07755.1,
RC ECO:0000313|Proteomes:UP000284120};
RA Zhang L.;
RT "Pedobacter endophyticus sp. nov., an endophytic bacterium isolated from a
RT leaf of Triticum aestivum.";
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 + 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:RWU07755.1}.
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DR EMBL; SAYW01000003; RWU07755.1; -; Genomic_DNA.
DR RefSeq; WP_113647665.1; NZ_QMHN01000003.1.
DR AlphaFoldDB; A0A443YV99; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000284120; 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 ECO:0000313|EMBL:RWU07755.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000284120}.
FT DOMAIN 4..153
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 184..306
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 307 AA; 34051 MW; EC5C8821F10A883C CRC64;
MKKILVVGIG GVGGYFGGRL AKSYQHSDEL AIYFLARGEN LSAIQANGLT VVEGNERFNT
KPHLATDDPT WIGPVDYVVL CIKNYDLDEC LLQLKPCIAE HTVILPLLNG VDHREKIQAA
YPQNLALAGC VYLVARLAAP GLVENTGKVS SLFFGHKDLK DDQLLWLAET LQQAGIEATL
TQEITQVIWR KFVFVSAIAT ATSFYHQSVG QIVEDQEMDR SLRQLIHEVC SLAKASNVGL
PDDIESLTYQ NLCKLPYATT SSMQVDRAKH AAKTELESLT GYVVHQMQQL KLPSPTFKLM
YDRLKQS
//
