ID I4CCJ7_DESTA Unreviewed; 343 AA.
AC I4CCJ7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 02-APR-2025, entry version 59.
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 OrderedLocusNames=Desti_4666 {ECO:0000313|EMBL:AFM27288.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfomonilia;
OC Desulfomonilales; Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM27288.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) 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 + NADPH + H(+);
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:ARBA00048793,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003360; AFM27288.1; -; Genomic_DNA.
DR RefSeq; WP_014812397.1; NC_018025.1.
DR AlphaFoldDB; I4CCJ7; -.
DR STRING; 706587.Desti_4666; -.
DR KEGG; dti:Desti_4666; -.
DR PATRIC; fig|706587.4.peg.5280; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_7; -.
DR OrthoDB; 5333395at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000006055; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
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:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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:UP000006055}.
FT DOMAIN 8..156
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 181..325
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 343 AA; 36913 MW; 6B962BB83B355740 CRC64;
MEHSQPKITV VGAGAIGGVT AAFLSRAGWN VEIICKRQEI AKQCSDPGLL ITGLRGESRT
PLHAVASIKE LSGPLQVVLL ATKATDCVSA ARELLPMLSD DGFVVSLQNG ICEEALAEVL
GRERLIGCVV AWGATMLGPG RLEVTSPGEF VIGNLDGKVD PRLDLLKEAL SSVAPTRISE
NIMGELYSKL IVNSCINTLG ALTGMTLGKL LASAQVRNIF MGLMTEAVAV ANAMNIRIEP
GGGGKLDYYK FLSGDGFWSR LRKHATVRVI GFKYRRIKSS SLQSLERGRP TEIDYLNGYI
CNKGREFSVP TPLNDAVTGM VKEIESGQRM ISPENVTDPR LRL
//
