ID A0A0M8VM13_9ACTN Unreviewed; 302 AA.
AC A0A0M8VM13;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=ADL00_14610 {ECO:0000313|EMBL:KOV68114.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV68114.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV68114.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV68114.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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:KOV68114.1}.
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DR EMBL; LGDU01000119; KOV68114.1; -; Genomic_DNA.
DR RefSeq; WP_053758570.1; NZ_LGDU01000119.1.
DR AlphaFoldDB; A0A0M8VM13; -.
DR PATRIC; fig|1519489.3.peg.3339; -.
DR OrthoDB; 4186253at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000037758; Unassembled WGS sequence.
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; 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 Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000037758}.
FT DOMAIN 8..145
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..293
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 302 AA; 31702 MW; 0293A3B6D300628F CRC64;
MAHDELTVAV LGPGGVGGLL AGLLARAGHR VICLAGETTA ETLRTTGVHV RSTLFGDFTA
DVEAAEELRE PVDVCLIAVK HTALDAALSR VPAHTLGDAL LVPFLNGIEH PSLLRSRYRP
DQVAPAVIRV ESTRVAPGEI EHASPFAEID LTGDPVPRER LDALAAAISA AGPTTRVLDD
EAAALWAKMS FLAPFALLTT RYALPLGDVR SRHRDELAAL VGETAAVSRA CGGPADPAQA
LARYDAFPPH TKSSMQRDAE AGRPLELDAI GGALLRAAER HGVPTPVAAK LVRELSYVTS
PT
//
