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Database: UniProt
Entry: A0A0K1XGB6_9GAMM
LinkDB: A0A0K1XGB6_9GAMM
Original site: A0A0K1XGB6_9GAMM 
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}.
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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
//
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