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Database: UniProt
Entry: U2E435_9GAMM
LinkDB: U2E435_9GAMM
Original site: U2E435_9GAMM 
ID   U2E435_9GAMM            Unreviewed;       295 AA.
AC   U2E435;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   Name=panE {ECO:0000313|EMBL:ERJ18606.1};
GN   ORFNames=SSPSH_002520 {ECO:0000313|EMBL:ERJ18606.1};
OS   Salinisphaera shabanensis E1L3A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Salinisphaera.
OX   NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18606.1, ECO:0000313|Proteomes:UP000006242};
RN   [1] {ECO:0000313|EMBL:ERJ18606.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18606.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=21705588; DOI=10.1128/JB.05459-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT   the harsh, variable environment of the brine-seawater interface of the
RT   Shaban Deep in the Red Sea.";
RL   J. Bacteriol. 193:4555-4556(2011).
RN   [2] {ECO:0000313|EMBL:ERJ18606.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18606.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC       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   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERJ18606.1}.
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DR   EMBL; AFNV02000017; ERJ18606.1; -; Genomic_DNA.
DR   RefSeq; WP_006914900.1; NZ_AFNV02000017.1.
DR   AlphaFoldDB; U2E435; -.
DR   STRING; 1033802.SSPSH_002520; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 6530772at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000006242; Unassembled WGS sequence.
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; 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   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:UP000006242}.
FT   DOMAIN          6..142
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          165..287
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   295 AA;  31859 MW;  231D874C02228514 CRC64;
     MPHWFLTGAG HIGTLAAYYL TRAGHDVSVL RNEAGAAIDA TLQFASDAST RRLTLPVRTP
     STCDRPIEYL IVACKTPYTP AALTRLDLGP NATVLRLQNG IGSLDGLLPD GARLIETVTT
     NAVNGTRNVH RVVAENQTWM GDGNTKPAWF DELARCWPGL VWERDIRTAQ WRKLVANAAI
     NALTALHDVP NGALLDDAQL YAQMRAIVAE TDQVLAALDE DWKASSLAAV ETVVQATAAN
     TSSMRADMQH GAVTEIDAIN GWLVEQGTRL GLDMTVNRTL VERVRALAPT RGSGE
//
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