ID R9T8H7_METII Unreviewed; 297 AA.
AC R9T8H7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 18-JUN-2025, entry version 58.
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=MMINT_02410 {ECO:0000313|EMBL:AGN25643.1};
OS Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC Archaea; Methanobacteriati; Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX NCBI_TaxID=1295009 {ECO:0000313|EMBL:AGN25643.1, ECO:0000313|Proteomes:UP000014070};
RN [1] {ECO:0000313|EMBL:AGN25643.1, ECO:0000313|Proteomes:UP000014070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Issoire-Mx1 {ECO:0000313|EMBL:AGN25643.1,
RC ECO:0000313|Proteomes:UP000014070};
RX PubMed=23846268; DOI=10.1128/genomeA.00453-13;
RA Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT human feces.";
RL Genome Announc. 1:142-142(2013).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of ketopantoate
CC into pantoic acid. {ECO:0000256|ARBA:ARBA00056765}.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NAD(+) = 2-dehydropantoate + NADH + H(+);
CC Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00048196};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC Evidence={ECO:0000256|ARBA:ARBA00048196};
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:ARBA00047506};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC Evidence={ECO:0000256|ARBA:ARBA00047506};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004724, 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; CP005934; AGN25643.1; -; Genomic_DNA.
DR RefSeq; WP_020448168.1; NC_021353.1.
DR AlphaFoldDB; R9T8H7; -.
DR STRING; 1295009.MMINT_02410; -.
DR GeneID; 41322679; -.
DR KEGG; mer:MMINT_02410; -.
DR HOGENOM; CLU_031468_6_1_2; -.
DR InParanoid; R9T8H7; -.
DR OrthoDB; 201845at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000014070; 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:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
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 Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993,
KW ECO:0000256|RuleBase:RU362068};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000014070}.
FT DOMAIN 3..148
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 171..291
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 297 AA; 31927 MW; 7B7DFEE96F0DE555 CRC64;
MNILVYGAGA IGSAIGEKLS GQHDVTLVSR KPHADAISSN GLLVCSSKGK ERVFLKCVTS
IDGMEPPDVI IVTTKAYDSK HAGDDISRII DDNTIIASIQ NGLGNYEHIS RRFGRKGVVG
TTTMGVTMTR PGEIVLAGEG VTSFGPYDDA AEKITDIFIK SGFEARTSSR IFSDIWMKAI
ANASINPITV ISGKTNGCIL YEPYMSLAKE ACYEAAAVAE AEGVMLDDPW KAVRDIAEKT
SSNKSSMLQD IEKGRKTEIN QITGEIVRRA GGIGIPVPIN SALLELIRSM EKKDKRL
//
