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Database: UniProt
Entry: D8JCV3_HALJB
LinkDB: D8JCV3_HALJB
Original site: D8JCV3_HALJB 
ID   D8JCV3_HALJB            Unreviewed;       304 AA.
AC   D8JCV3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 89.
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=HacjB3_17528 {ECO:0000313|EMBL:ADJ16848.1};
GN   ORFNames=C497_07239 {ECO:0000313|EMBL:ELY38716.1};
OS   Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS   4019 / B3).
OG   Plasmid 2 {ECO:0000313|EMBL:ADJ16848.1, ECO:0000313|Proteomes:UP000000390}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halalkalicoccus.
OX   NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ16848.1, ECO:0000313|Proteomes:UP000000390};
RN   [1] {ECO:0000313|EMBL:ADJ16848.1, ECO:0000313|Proteomes:UP000000390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|EMBL:ADJ16848.1}, and DSM 18796 / CECT 7217 /
RC   JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RC   PLASMID=2 {ECO:0000313|Proteomes:UP000000390};
RX   PubMed=20601480; DOI=10.1128/JB.00663-10;
RA   Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT   "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT   halophilic archaeon.";
RL   J. Bacteriol. 192:4528-4529(2010).
RN   [2] {ECO:0000313|Proteomes:UP000011645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY38716.1, ECO:0000313|Proteomes:UP000011645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|EMBL:ELY38716.1,
RC   ECO:0000313|Proteomes:UP000011645};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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DR   EMBL; CP002064; ADJ16848.1; -; Genomic_DNA.
DR   EMBL; AOHV01000020; ELY38716.1; -; Genomic_DNA.
DR   RefSeq; WP_008415607.1; NZ_AXZD01000022.1.
DR   AlphaFoldDB; D8JCV3; -.
DR   GeneID; 9421295; -.
DR   KEGG; hje:HacjB3_17528; -.
DR   PATRIC; fig|795797.18.peg.3421; -.
DR   eggNOG; arCOG04139; Archaea.
DR   HOGENOM; CLU_031468_0_0_2; -.
DR   OMA; WEKLAFN; -.
DR   OrthoDB; 201845at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000390; Plasmid 2.
DR   Proteomes; UP000011645; Unassembled WGS sequence.
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};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068}; Plasmid {ECO:0000313|EMBL:ADJ16848.1}.
FT   DOMAIN          3..150
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          178..299
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   304 AA;  33151 MW;  826998683C3B283F CRC64;
     MNIAVIGAGA LGCLFGGRLT ESGHDVYLLH YRQAYVDHLN EAGLTIESEN DEKTDIAVTA
     TTDANEIGVA DLVIVFVKSH QTRDALAEHA ACIGPETDLL SLQNGLRHYD RLLDIADEDH
     SFAGVTYQGA VVEEPGYIRV TSSGSSTFGG ANDGGLHRIE EILVEAGFPV ELVDDPRPYI
     WAKQLVSLPI KPLAALTHLS NGELIETPET RTLMKEIVAE AEYVAEHHGV DIPMDDPMAE
     VVATCEESYS HYSSMLQDIR AKRKTEIDDV NGAIVDIARE EDVDVPINEL ATNLVRALEK
     SYLD
//
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