ID V5SCX4_9HYPH Unreviewed; 311 AA.
AC V5SCX4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 18-JUN-2025, entry version 49.
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=W911_08185 {ECO:0000313|EMBL:AHB48373.1};
OS Hyphomicrobium nitrativorans NL23.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=1029756 {ECO:0000313|EMBL:AHB48373.1, ECO:0000313|Proteomes:UP000018542};
RN [1] {ECO:0000313|EMBL:AHB48373.1, ECO:0000313|Proteomes:UP000018542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL23 {ECO:0000313|EMBL:AHB48373.1};
RX PubMed=24435868;
RA Martineau C., Villeneuve C., Mauffrey F., Villemur R.;
RT "Complete Genome Sequence of Hyphomicrobium nitrativorans Strain NL23, a
RT Denitrifying Bacterium Isolated from Biofilm of a Methanol-Fed
RT Denitrification System Treating Seawater at the Montreal Biodome.";
RL Genome Announc. 2:e01165-13(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 + 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}.
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DR EMBL; CP006912; AHB48373.1; -; Genomic_DNA.
DR RefSeq; WP_023787017.1; NC_022997.1.
DR AlphaFoldDB; V5SCX4; -.
DR STRING; 1029756.W911_08185; -.
DR KEGG; hni:W911_08185; -.
DR PATRIC; fig|1029756.8.peg.1706; -.
DR HOGENOM; CLU_031468_6_1_5; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000018542; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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 NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000018542}.
FT DOMAIN 3..140
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..297
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 311 AA; 33274 MW; C248428F6F30E742 CRC64;
MRVLIVGAGG VGGYIGARLV AAGMDVMFVV REARRAQLAA HGLVVESPLG NFSGAVAAVG
SPSSGFSPDV AIVACKAHAL DRALDVVDAG RGPHTRILPL LNGVAHLDVL RRRFPDVPVL
GGLVHGALTL REDGVVAHLT PFFSAIVGTE TGAPDAVAEE FVRRLSAAHV DVRLSPDIRQ
DMWNKFVFLA TFAGITCLMR ASIGTIMCAD GGEDITLQLL DECLAVSRAE GFAPDEASMS
SYRRVLTEPG STFTSSMLRD ILSGHRTEAD HIVGDMLRRA RRHRIDTPML KIALAHLQCF
EATVRHNERT L
//
