GenomeNet

Database: UniProt
Entry: F8AIU9_PYRYC
LinkDB: F8AIU9_PYRYC
Original site: F8AIU9_PYRYC 
ID   F8AIU9_PYRYC            Unreviewed;       327 AA.
AC   F8AIU9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014, 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   OrderedLocusNames=PYCH_07360 {ECO:0000313|EMBL:AEH24424.1};
OS   Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24424.1, ECO:0000313|Proteomes:UP000008386};
RN   [1] {ECO:0000313|EMBL:AEH24424.1, ECO:0000313|Proteomes:UP000008386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX   PubMed=21705594; DOI=10.1128/JB.05345-11;
RA   Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT   "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT   archaeon Pyrococcus yayanosii CH1.";
RL   J. Bacteriol. 193:4297-4298(2011).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000256|ARBA:ARBA00000108};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC         Evidence={ECO:0000256|ARBA:ARBA00000108};
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:ARBA00000825};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC         Evidence={ECO:0000256|ARBA:ARBA00000825};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004724, ECO:0000256|RuleBase:RU362068}.
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; CP002779; AEH24424.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8AIU9; -.
DR   STRING; 529709.PYCH_07360; -.
DR   KEGG; pya:PYCH_07360; -.
DR   eggNOG; arCOG04139; Archaea.
DR   HOGENOM; CLU_031468_0_1_2; -.
DR   OMA; NYSSMYQ; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000008386; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 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   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993,
KW   ECO:0000256|RuleBase:RU362068}; Membrane {ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..162
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          190..311
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   327 AA;  35440 MW;  E235525FAC44BD12 CRC64;
     MTKGIKDPRG KLSGIAMKIY VLGAGAIGSL FGALLARAGN DVLLVGRRPH VEAIQRDGLK
     VIGVEEFTVD IDAAVEIPEE PPDLIVLATK SYSTAEALEA AKKAIGERTW IMSIQNGLGN
     EEKALKYTKN VIGAVTTNGA MLEAPGRVKW TGKGITVLGL YPRGRHPFVE EVKEEMRRAG
     LEAFVTENAA GWKWAKAIVN SAVNPIGALL EVKNGYLLEN ESLLSIVMEV VKEGCRVALQ
     NGIEFEVPPM ELLFQTLERT RENYNSMLQD IWRGKRTEVD YINGKIVEYA GAVGLEAPMN
     ELLWALIRGK EALAAGGKNA DTGRKGG
//
DBGET integrated database retrieval system