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Database: UniProt
Entry: A0A1E7RIT0_9GAMM
LinkDB: A0A1E7RIT0_9GAMM
Original site: A0A1E7RIT0_9GAMM 
ID   A0A1E7RIT0_9GAMM        Unreviewed;       312 AA.
AC   A0A1E7RIT0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=BIY45_18715 {ECO:0000313|EMBL:OEY99107.1};
OS   Stenotrophomonas sp. BIIR7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEY99107.1, ECO:0000313|Proteomes:UP000175905};
RN   [1] {ECO:0000313|EMBL:OEY99107.1, ECO:0000313|Proteomes:UP000175905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIIR7 {ECO:0000313|EMBL:OEY99107.1,
RC   ECO:0000313|Proteomes:UP000175905};
RA   Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P., Busse H.J.,
RA   Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT   "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT   formations.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:OEY99107.1}.
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DR   EMBL; MKCZ01000134; OEY99107.1; -; Genomic_DNA.
DR   RefSeq; WP_070209487.1; NZ_MKCZ01000134.1.
DR   AlphaFoldDB; A0A1E7RIT0; -.
DR   STRING; 1904462.BIY45_18715; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000175905; 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; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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|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:UP000175905}.
FT   DOMAIN          3..155
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..307
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   312 AA;  32194 MW;  A2693C1964069277 CRC64;
     MRILVLGAGG TGGYFGGRLA QTGLDVTFLV RPVRAAQLDQ DGLVIRSPLG DAAFPVAHVT
     ADALPALAAE QPFDLVMLSC KAYDLESSIE AIAPAVSSRT TVLPILNGLR HYAALDARFG
     RDAVLGGLCF ISATKADDGA VLHLAPAAKI TFGERDTPGS SARVLALAAA CVQAGVDHVA
     SEAIGKEQWV KYTFLTALAA ATCVMRADVG MIVATDDGAA VVRGLYDECL AVAEAAGEPV
     PEKARTIALS ALTQEGSALK ASMLRDLEAG QQVEAEQIVG DMLARARAAG QAAPLLAVAY
     AHLQAYQRSR AG
//
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