ID A0A4Q9HJH0_STRKA Unreviewed; 305 AA.
AC A0A4Q9HJH0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
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};
DE Flags: Fragment;
GN ORFNames=EYS09_36495 {ECO:0000313|EMBL:TBO54826.1};
OS Streptomyces kasugaensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1946 {ECO:0000313|EMBL:TBO54826.1, ECO:0000313|Proteomes:UP000292452};
RN [1] {ECO:0000313|EMBL:TBO54826.1, ECO:0000313|Proteomes:UP000292452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-2504 {ECO:0000313|EMBL:TBO54826.1,
RC ECO:0000313|Proteomes:UP000292452};
RA Napolioni V., Giuliodori A.M., Spurio R., Fabbretti A.;
RT "Draft Genome Sequence of Streptomyces sp. AM-2504, identified by 16S rRNA
RT comparative analysis as a Streptomyces Kasugaensis strain.";
RL Submitted (FEB-2019) 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|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:TBO54826.1}.
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DR EMBL; SIXH01000688; TBO54826.1; -; Genomic_DNA.
DR RefSeq; WP_131126419.1; NZ_SIXH01000688.1.
DR AlphaFoldDB; A0A4Q9HJH0; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000292452; 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:TBO54826.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000292452}.
FT DOMAIN 18..154
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 190..302
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT NON_TER 305
FT /evidence="ECO:0000313|EMBL:TBO54826.1"
SQ SEQUENCE 305 AA; 31822 MW; D76EE8E585957B44 CRC64;
MRTTSPLTDT PAPHRWTVAV LGPGGVGGLL AGLLSRAGHR VICVAGEDTA RALRQDGIRV
RSGQFGDFTA PVEADTALRE PVGLCLVTVK HTALTAALER VPPQVLGDGL VLPLLNGVEH
PAALRERYGA RRVVAGTIRV ESTRIAPGTI EHGSPFTEID LTGTADRLGP LTAMFEDAGV
RTRPVADETA ALWAKLTFLA PFALLTTRYG LTLGEVRTGR RAELAALVAE AAAVSGACGV
PADPARTLAR YDTFPAGAKS SMQRDAEAGR PLELDAIGGA LLRAAERHGV PTPVVGRLMS
ELMAG
//
