ID A0A1Z5IIK7_9LACO Unreviewed; 334 AA.
AC A0A1Z5IIK7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=apbA_5 {ECO:0000313|EMBL:GAX01607.1};
GN ORFNames=IWT126_01650 {ECO:0000313|EMBL:GAX01607.1};
OS Secundilactobacillus silagei JCM 19001.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302250 {ECO:0000313|EMBL:GAX01607.1, ECO:0000313|Proteomes:UP000198402};
RN [1] {ECO:0000313|EMBL:GAX01607.1, ECO:0000313|Proteomes:UP000198402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IWT126 {ECO:0000313|EMBL:GAX01607.1,
RC ECO:0000313|Proteomes:UP000198402};
RA Tohno M., Tanizawa Y., Arita M.;
RT "Draft genome sequences of new species of the genus Lactobacillus isolated
RT from orchardgrass silage.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC 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|ARBA:ARBA00000784,
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:GAX01607.1}.
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DR EMBL; BCMG01000008; GAX01607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5IIK7; -.
DR STRING; 1302250.GCA_001313225_02444; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000198402; 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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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}.
FT DOMAIN 4..149
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 190..311
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 334 AA; 38274 MW; D2EF22A7FE257611 CRC64;
MKYGIIGAGA MGYRYGVMLQ ENAGVDVDFI DTWEPNVKKV REQGGVSVAR DHKNRRIIPI
NMYYPEEYTG HPDVWIIFKK QMQLAEELKR DSKAGIFHDD QYVFSAMNGM GHFEKIEKYF
PKDHIICGTA MIATRLDGPA NVDFMGPVNS EVMHMAPYNN KPADKTTEAV FNDFTAAKMG
PVMVDEWKGM CMSKVVFNAV TNTLCTMFEM QMGQFIEYEG VTKMATTLFN EAFDACERAG
IHMIESRQEE IDSVIPVSQA YKYHYPSMYQ DFSKGRPTEV DYINGYIAKI GREHDYVCRV
HEFVVQEVHM AEMMRKYHKP QENVADSKKA QVEA
//
