ID A0A1M4XWA4_9BACL Unreviewed; 309 AA.
AC A0A1M4XWA4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, 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};
GN ORFNames=SAMN05444392_105219 {ECO:0000313|EMBL:SHE97759.1};
OS Seinonella peptonophila.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Seinonella.
OX NCBI_TaxID=112248 {ECO:0000313|EMBL:SHE97759.1, ECO:0000313|Proteomes:UP000184476};
RN [1] {ECO:0000313|EMBL:SHE97759.1, ECO:0000313|Proteomes:UP000184476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44666 {ECO:0000313|EMBL:SHE97759.1,
RC ECO:0000313|Proteomes:UP000184476};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQVL01000005; SHE97759.1; -; Genomic_DNA.
DR RefSeq; WP_073154824.1; NZ_FQVL01000005.1.
DR AlphaFoldDB; A0A1M4XWA4; -.
DR STRING; 112248.SAMN05444392_105219; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000184476; 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:UP000184476}.
FT DOMAIN 3..152
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..301
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 309 AA; 34492 MW; 34B5F1F9599EEBBC CRC64;
MRVGIVGAGA VGGYFGGRLA EKGADVTFLV RPNRKKRLTE KGLVIHSPIH GNSHRSVSVV
TPEETAPPFD LLIVAVKAYH LDSVIPFMQT FSDQHTMILP LLNGYAHIDH LQQAFSKDSI
FGGFCFMEST LDQSGEIHLL GKHHRLVYGE LQENANHARM DQLKQLFADA NLEAVQSDFI
ETEMWNKYQY IAALSGMTTL MRSEIGAIRD STYGSELYQQ LLNEIYQVTI RQPLPKPPES
PDIIWNRVQK ASPQSTSSMY RDLKQGLPIE TDHLHGSLVR WGKEANLSLP ILTTIYTGLS
LYQPSGSSL
//
