ID A0A259UVE4_9FIRM Unreviewed; 339 AA.
AC A0A259UVE4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=SPACI_16650 {ECO:0000313|EMBL:OZC21982.1};
OS Sporomusa acidovorans DSM 3132.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC21982.1, ECO:0000313|Proteomes:UP000216052};
RN [1] {ECO:0000313|EMBL:OZC21982.1, ECO:0000313|Proteomes:UP000216052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC21982.1,
RC ECO:0000313|Proteomes:UP000216052};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL Submitted (FEB-2016) 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:OZC21982.1}.
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DR EMBL; LSLL01000048; OZC21982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259UVE4; -.
DR STRING; 112900.SAMN04488499_106512; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000216052; 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:UP000216052}.
FT DOMAIN 4..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..318
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 339 AA; 36652 MW; 4538BEBC33900A4B CRC64;
MRMAVMGAGS LGTILGALLA KNGYDVDLID VNIAHVKALN EGGAQIVGLM DLVQPVKALT
PEEMHEQYDI IFYLVKATYN EGALPYVNKY LKSNGVVVVG QNGLPEEAVA AVVGKNRVIG
QITGWGATWM ESGVSKLTSQ PDHMTYHIGE LDGKVTERLK KVADILSKAG KPEIVTNLMG
IRWTKMTSNC CFSGMSAVVA GNFGDVIDNP KAVRCSAHIL NESMAIAKAA GVKPEVFQGD
DFTKLTFETE KELEIKVPGI RAIVESHRNI RTGILYDIEA GRYPEVDTTF NGNLCRLGAK
YGVSTPVNQQ VTDIIRALAN GKLKIDPANV DRIELPKLP
//
