ID A0A0K1XGB6_9GAMM Unreviewed; 305 AA.
AC A0A0K1XGB6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AKN88_09920 {ECO:0000313|EMBL:AKX60208.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX60208.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX60208.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX60208.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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|ARBA:ARBA00000784,
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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; CP012365; AKX60208.1; -; Genomic_DNA.
DR RefSeq; WP_053101513.1; NZ_JACANE010000006.1.
DR AlphaFoldDB; A0A0K1XGB6; -.
DR STRING; 1697053.AKN87_00405; -.
DR PATRIC; fig|1698449.3.peg.1994; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000063953; Chromosome.
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; PTHR43765:SF3; 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:UP000063953}.
FT DOMAIN 10..157
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..299
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 305 AA; 33701 MW; F51AA3F76A80197F CRC64;
MNTGVSTIHW HILGAGSLGC LWAARLAQVK QSVHLILRSA VRLQAFPGQV QLTTQHTCQS
LALTAELADT SQTPITHLIV ACKAYDALTA IDSIAPRLAE NACIILLQNG LGSQQAIIQR
YSKQRIIAAS TTDGAYLTAP FQVTWAGQGL TQLGDLNHLG QAAPHWLELW QVAGIHNQWN
PQIWHALWLK LAVNCAINPL TVLHQCRNGE LRQQASQVNA LIPELTLLLK QAEVPLQPNQ
LHQLIWQVIE QTANNTSSML QDVQQQRPTE AEFITGFACH YARSQQLTVP HLNALHHALI
EQLTY
//