ID A0A0E3YTW7_9BACT Unreviewed; 312 AA.
AC A0A0E3YTW7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=IMCC26134_07880 {ECO:0000313|EMBL:AKC82714.1};
OS Verrucomicrobia bacterium IMCC26134.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1637999 {ECO:0000313|EMBL:AKC82714.1, ECO:0000313|Proteomes:UP000033046};
RN [1] {ECO:0000313|EMBL:AKC82714.1, ECO:0000313|Proteomes:UP000033046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26134 {ECO:0000313|EMBL:AKC82714.1,
RC ECO:0000313|Proteomes:UP000033046};
RA Choi A., Kang I., Cho J.-C.;
RT "Complete genome sequence of Verrucomicrobia strain IMCC26134.";
RL Submitted (APR-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}.
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DR EMBL; CP011265; AKC82714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3YTW7; -.
DR STRING; 1637999.IMCC26134_07880; -.
DR KEGG; vba:IMCC26134_07880; -.
DR PATRIC; fig|1637999.3.peg.1715; -.
DR HOGENOM; CLU_031468_6_1_0; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000033046; Chromosome.
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:UP000033046}.
FT DOMAIN 8..155
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..300
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 312 AA; 33008 MW; 213CB813289B9D53 CRC64;
MFPVHPRIAV VGSGALGLYY GGRLARSGHD VVFLARADLD VIRANGVTVS YPGERYTLHP
VRVAAKPAEI GPVDLVIIGL KATANEALPL LLPPLLGPET VVVNLQNGLG VDEQVAAVSG
AAHVVGALCF VCVNRTAPGV AECTLPGYIA LGELAGGLTD RTSAVAELFT QAGLKTQLAG
SLLAARWHKL VWNIPFNGLA VVSGVVRAGM TTDRILQDPV LEARVWALMR EVQSIARAEG
VAIADEFVVK QVEQTRPMGP YKPSTMVDYV AGRPLEITPI WGEPLRRAQA LGVAAPELYK
LHEELCLAGV KV
//