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Database: UniProt
Entry: F3L1R8_9GAMM
LinkDB: F3L1R8_9GAMM
Original site: F3L1R8_9GAMM 
ID   F3L1R8_9GAMM            Unreviewed;       294 AA.
AC   F3L1R8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=EYZ66_10575 {ECO:0000313|EMBL:QHJ88706.1}, IMCC3088_1408
GN   {ECO:0000313|EMBL:EGG29771.1};
OS   Aequoribacter fuscus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Aequoribacter.
OX   NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG29771.1, ECO:0000313|Proteomes:UP000005615};
RN   [1] {ECO:0000313|EMBL:EGG29771.1, ECO:0000313|Proteomes:UP000005615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG29771.1,
RC   ECO:0000313|Proteomes:UP000005615};
RX   PubMed=21551310; DOI=10.1128/JB.05111-11;
RA   Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT   "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT   bacterium belonging to the OM60/NOR5 clade.";
RL   J. Bacteriol. 193:3415-3416(2011).
RN   [2] {ECO:0000313|EMBL:QHJ88706.1, ECO:0000313|Proteomes:UP000464557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3088 {ECO:0000313|EMBL:QHJ88706.1,
RC   ECO:0000313|Proteomes:UP000464557};
RA   Li S.-H.;
RT   "Halieaceae_genomes.";
RL   Submitted (FEB-2019) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR   EMBL; AEIG01000034; EGG29771.1; -; Genomic_DNA.
DR   EMBL; CP036423; QHJ88706.1; -; Genomic_DNA.
DR   RefSeq; WP_009575703.1; NZ_CP036423.1.
DR   AlphaFoldDB; F3L1R8; -.
DR   STRING; 2518989.IMCC3088_1408; -.
DR   KEGG; afus:EYZ66_10575; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 6530772at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000005615; Unassembled WGS sequence.
DR   Proteomes; UP000464557; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF3; 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|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:UP000005615}.
FT   DOMAIN          6..146
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          167..283
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   294 AA;  32634 MW;  1F891B34B54C87F2 CRC64;
     MSNPPWHILG FGVIGQLLHA GFSRSGQQCL VVSKPNQPLP AHHTVQYQNH TETFDIEVFV
     PGDRLIERLV VCTKSYDVTQ AITAVKQALS PTAQIVIMVN GLVDSHEIAE LTTGSVYWAL
     TTEGGYRNEA HHTVHGGSGV TRLGSGSEPD WLREWQEAVP NSHWHTDIDP YRWEKLSVNA
     VINPLTALHQ CRNGELENSE LKACTQTSID EARAVLEALG FTLQAQGFHN TCWEVIRKTG
     ANRSSMLQDI TLKRRTEIST ILPPLLAVAA KHHVATPQLK NTLTAFQQRF PELC
//
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