ID V7I015_9CLOT Unreviewed; 303 AA.
AC V7I015;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=T472_0218220 {ECO:0000313|EMBL:ETA79218.1};
OS Youngiibacter fragilis 232.1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Youngiibacter.
OX NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA79218.1, ECO:0000313|Proteomes:UP000017747};
RN [1] {ECO:0000313|EMBL:ETA79218.1, ECO:0000313|Proteomes:UP000017747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232.1 {ECO:0000313|EMBL:ETA79218.1,
RC ECO:0000313|Proteomes:UP000017747};
RX PubMed=24459265;
RA Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT Youngiibacter.";
RL Genome Announc. 2:e01183-13(2014).
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}.
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:ETA79218.1}.
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DR EMBL; AXUN02000222; ETA79218.1; -; Genomic_DNA.
DR RefSeq; WP_023383448.1; NZ_AXUN02000222.1.
DR AlphaFoldDB; V7I015; -.
DR STRING; 994573.T472_0218220; -.
DR PATRIC; fig|994573.3.peg.3461; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9772736at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000017747; 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:UP000017747}.
FT DOMAIN 4..141
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 179..291
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 303 AA; 32829 MW; 7B89748D2D328E1A CRC64;
MRYLVIGAGG TGGSIAAYMN EAGRDVTVIA RGRHLEAIKD KGLRMETPDR GSFLSKPKAS
DMENYSERPD AIFVCVKGYS LEESIPFIRK VSGPDTVVIP ILNIYGTGGR MQEKLPGVLV
TDGCIYIAAE ISEPGTIIKK SDGIKVVFGT RKPEEYRDVL KVIRADLEES GIISMLSDNI
TRDTFQKFAF ISPFAACGAY YDVAAEELQK DGVSRDMFAA LTKEVLSIAE GMGITFGSDI
VKSNLDFIDS LSPSATASMQ RDLKKGGDSE IDGLVFEVVR MGRTLGVDVP EYVKVSAKFG
FGI
//
