ID A0A829YMT5_9GAMM Unreviewed; 327 AA.
AC A0A829YMT5;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=GCM10011487_61620 {ECO:0000313|EMBL:GFE84162.1};
OS Steroidobacter agaridevorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Steroidobacterales; Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=2695856 {ECO:0000313|EMBL:GFE84162.1, ECO:0000313|Proteomes:UP000445000};
RN [1] {ECO:0000313|Proteomes:UP000445000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YU21-B {ECO:0000313|Proteomes:UP000445000};
RA Ikenaga M., Kataoka M., Murouchi A., Katsuragi S., Sakai M.;
RT "'Steroidobacter agaridevorans' sp. nov., agar-degrading bacteria isolated
RT from rhizosphere soils.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:GFE84162.1}.
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; BLJN01000008; GFE84162.1; -; Genomic_DNA.
DR RefSeq; WP_161815769.1; NZ_BLJN01000008.1.
DR AlphaFoldDB; A0A829YMT5; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000445000; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 FunFam; 3.40.50.720:FF:000307; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005089; PRK06522.1-4; 1.
DR PANTHER; PTHR21708:SF45; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000445000}.
FT DOMAIN 3..168
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 327 AA; 34223 MW; 36294F038A7EBD13 CRC64;
MRIAIVGAGA IGIWLGARLA NAGQDVSVLA RGETLAAVRE HGLRLAIGGN MQAAAVTVSD
RASDLGKQDL VVLAVKGQAL SSVADSVAAL LDEETMILPA MNGIPWWFFH GLPVSLDDTS
LRSVDPDGRV TQSMPPERVL GCVVHASCSV QAPGYSVHTK GNGLIVGEPR GGTSARLDAA
VNALRAAGFD VTVSPQIQKD IWYKLWGNMT MNPISALTAA TSDLILDDPL VSGFILRVMA
EAAAIGARIG CPIAESGEDR MAVTRKLGAF KTSMLQDAEA GRSLEIDALV AAPREIGRRV
GIETPNMDAL HGLIRLFASA RRNTASS
//
