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Entry: A0A1I2FD21_9BACT
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ID   A0A1I2FD21_9BACT        Unreviewed;       314 AA.
AC   A0A1I2FD21;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   18-JUN-2025, entry version 22.
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=SAMN05216283_102427 {ECO:0000313|EMBL:SFF02460.1};
OS   Sunxiuqinia elliptica.
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Marinilabiliales;
OC   Prolixibacteraceae; Sunxiuqinia.
OX   NCBI_TaxID=655355 {ECO:0000313|EMBL:SFF02460.1, ECO:0000313|Proteomes:UP000198964};
RN   [1] {ECO:0000313|EMBL:SFF02460.1, ECO:0000313|Proteomes:UP000198964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFF02460.1,
RC   ECO:0000313|Proteomes:UP000198964};
RA   de Groot N.N.;
RL   Submitted (OCT-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 + 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; FONW01000002; SFF02460.1; -; Genomic_DNA.
DR   RefSeq; WP_093919088.1; NZ_FONW01000002.1.
DR   AlphaFoldDB; A0A1I2FD21; -.
DR   STRING; 655355.SAMN05216283_102427; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000198964; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; IPR013752; KPA_reductase.
DR   InterPro; IPR051402; KPR-Related.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   NCBIfam; NF004887; PRK06249.1; 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|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198964}.
FT   DOMAIN          6..150
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          181..299
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   314 AA;  34810 MW;  6DD0CBE3BB984FAC CRC64;
     MKLKYGVVGT GALGGFYGGK LAKAGHDVHF LLRSDFEHVK EQGLKVDSVD GDFLLQPIAC
     YNSAQDMPVC DVVLVCMKTT GNHLLPELLD PIIDEQSLVI LVQNGLGIEE RLAQEVPHAS
     VAGGIAFICA HKVGPGHVSH LDLGRLILGL HTSTGNELLQ QCQQDFEQAG VPAQLAENLG
     YIRWQKLVWN VPFNGLAVVL NTTTDQLMKQ KETRELAHEM MHEVIFGAKN CGYDLDPDFA
     DKMIRTTEKM TPYAPSMKLD FDNRRAMEIE SIYTSPVQAA RQAGFEMKKV AMLESQLRFI
     ASQMENWKIR VSEG
//
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