ID A0A5B7YDL4_9ALTE Unreviewed; 346 AA.
AC A0A5B7YDL4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 21.
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=FBQ74_10110 {ECO:0000313|EMBL:QCZ93817.1};
OS Salinimonas iocasae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
OC Salinimonas.
OX NCBI_TaxID=2572577 {ECO:0000313|EMBL:QCZ93817.1, ECO:0000313|Proteomes:UP000304912};
RN [1] {ECO:0000313|EMBL:QCZ93817.1, ECO:0000313|Proteomes:UP000304912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KX18D6 {ECO:0000313|EMBL:QCZ93817.1,
RC ECO:0000313|Proteomes:UP000304912};
RA Zhang H., Wang H., Li C.;
RT "Salinimonas iocasae sp. nov., a halophilic bacterium isolated from the
RT outer tube casing of tubeworms in Okinawa Trough.";
RL Submitted (APR-2019) 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}.
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DR EMBL; CP039852; QCZ93817.1; -; Genomic_DNA.
DR RefSeq; WP_139756560.1; NZ_CP039852.1.
DR AlphaFoldDB; A0A5B7YDL4; -.
DR KEGG; salk:FBQ74_10110; -.
DR OrthoDB; 6530772at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000304912; 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|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000304912}.
FT DOMAIN 4..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 173..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 346 AA; 38156 MW; 83225FC133CCC868 CRC64;
MTHLVFGAGL VGSYLAGVLA INGYRTTAIG RDTQLSALAA GVKLSDFLGN HATAPAVTAF
NQHNDDAPEV IWLTVKCTDL TRAAQALKSV TGPKTSIVCC QNGLRAAHQI RAALPGRKVF
SAVVPFNVVR LDDGTLHRGS EGPLTLPREI KRVLPGFSGA MQHPLLSLRF TSDISAVQAA
KLQLNLSNAV NALSDLPVKT MLEDRGYRKI IAELMREWLE VASVNRIAVA KVTRIDGKWL
PFLLCLPNFL FRRVARKMLD IDPTVRTSMW WDLQRGKATE IEDLNGEVVR QGVIARNYCP
ANKVIIDLIH DAEKQRRETG RYAAMSASEL HNEIEIKRLE KSSYKI
//
