ID I8UDW6_9BACI Unreviewed; 298 AA.
AC I8UDW6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=A374_11815 {ECO:0000313|EMBL:EIT84983.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT84983.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT84983.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT84983.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
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:EIT84983.1}.
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DR EMBL; AKKV01000027; EIT84983.1; -; Genomic_DNA.
DR RefSeq; WP_007202443.1; NZ_AKKV01000027.1.
DR AlphaFoldDB; I8UDW6; -.
DR STRING; 1196324.A374_11815; -.
DR PATRIC; fig|1196324.3.peg.2418; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000004080; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000004080}.
FT DOMAIN 3..147
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..294
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 298 AA; 33306 MW; 9E21920F7951A513 CRC64;
MKVAVIGGGA IGLLMASMLT EMGSNVTLYT RTEEQANAIM KRGVKCHYFG KNERYYPLHA
RKFPDLKEEA DLVVICVKQH QLSSVLAFLK QSAMVRHAIP LFLQNGMGHL SSIEQLPQSV
VMAGVVEHGA LRISETDVQQ TGKGALRLFF VKGNNQDVQR YLQHPILDAV FSENARHTME
EKLLANAVIN PLTALFEVEN GALLHNESLR TLALMLFEEA RSVLNRSDRE KDLAYLWNIC
EGTKRNRSSM LKDIENGTPT EIEAISGYLI KQAEAQNLPV PYTSFVYHAI KAKELVIP
//