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Database: UniProt
Entry: A0A7L7KR11_9BACT
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ID   A0A7L7KR11_9BACT        Unreviewed;       343 AA.
AC   A0A7L7KR11;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   02-APR-2025, entry version 15.
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=G4Z02_02450 {ECO:0000313|EMBL:QMS84656.1};
OS   Candidatus Xianfuyuplasma coldseepsis.
OC   Bacteria; Bacillati; Mycoplasmatota; Candidatus Izimaplasma;
OC   Candidatus Izemoplasmatales; Candidatus Izemoplasmataceae;
OC   Candidatus Xianfuyuplasma.
OX   NCBI_TaxID=2782163 {ECO:0000313|EMBL:QMS84656.1, ECO:0000313|Proteomes:UP000514720};
RN   [1] {ECO:0000313|EMBL:QMS84656.1, ECO:0000313|Proteomes:UP000514720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zrk13 {ECO:0000313|Proteomes:UP000514720};
RA   Zheng R.K., Sun C.M.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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 + NADPH + H(+);
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:ARBA00048793,
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}.
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DR   EMBL; CP048914; QMS84656.1; -; Genomic_DNA.
DR   RefSeq; WP_258878275.1; NZ_CP048914.1.
DR   AlphaFoldDB; A0A7L7KR11; -.
DR   KEGG; xcl:G4Z02_02450; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000514720; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
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:SF2; 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:UP000514720}.
FT   DOMAIN          3..139
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          179..321
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   343 AA;  37703 MW;  FD056F4EFE9DE418 CRC64;
     MRVAIYGAGA MGTVLGAFIT KAGYEVDLIN RNKDHVRGLQ EHGAQIQGTL SMSQDVTALL
     PEEMTGLYDV ILLMTKQRHN QEIVTFLQPY LAQDGVLCTL QNGIPEPLIA SIIGDERTIG
     ATMSWGATFI GGGVVELTTE PSRETLTFSI GSYSDKRPQH FDYVVTLLHT MGHVTIEDNF
     IGARWSKLLI NAAYSGLSVV TGATFGELNK NRTTRTIALG AMKECIDVAK ASNLMIEPLQ
     GKDVVKLMDY NNPFKKQFSL FLLPIAMRKH KNIKSSMLRD LARGYTTEID AINGVVCDAG
     DQVGIETPIN DLIVSIVHEI ETNKRASSWD NIKDFDMMNM KGA
//
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