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Database: UniProt
Entry: A4XDX8_NOVAD
LinkDB: A4XDX8_NOVAD
Original site: A4XDX8_NOVAD 
ID   A4XDX8_NOVAD            Unreviewed;       337 AA.
AC   A4XDX8;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
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   OrderedLocusNames=Saro_3896 {ECO:0000313|EMBL:ABP64139.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OG   Plasmid pNL1 {ECO:0000313|EMBL:ABP64139.1,
OG   ECO:0000313|Proteomes:UP000009134}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABP64139.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|EMBL:ABP64139.1, ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RC   PLASMID=pNL1 {ECO:0000313|EMBL:ABP64139.1,
RC   ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT   "Complete sequence of plasmid pNL1 of Novosphingobium aromaticivorans DSM
RT   12444.";
RL   Submitted (APR-2007) 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}.
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DR   EMBL; CP000676; ABP64139.1; -; Genomic_DNA.
DR   RefSeq; WP_010890875.1; NC_009426.1.
DR   AlphaFoldDB; A4XDX8; -.
DR   KEGG; nar:Saro_3896; -.
DR   HOGENOM; CLU_031468_0_0_5; -.
DR   OMA; ITHAQSK; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000009134; Plasmid pNL1.
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|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW   Plasmid {ECO:0000313|EMBL:ABP64139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT   DOMAIN          8..159
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          185..333
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   337 AA;  36198 MW;  1FEB0BEF596B7FE0 CRC64;
     MSKQLHFCFH GAGGLGSVIG GFLARGGHKV TLIARKPHVE AIRRDGLSIS GVRAQFVQRE
     NLFAVETPEE VEGDIDYYIL LTKAKGTDQA LADAQVLVDR TACALTLQNG VGKEGKLQAA
     FGKDKVIGGS IMDGATLLEP GKALNHMAVP VTAYFGELEG GESERTRIMA EALDAAGMGS
     RSTPDIVHVH WEKVVQVGGA SSWSASTLGA LPKLDFVDGV AVREGAEHYV HVVKDLLAIY
     KALGYEPQNY FAPVSRLVEI DREGFEEAVS GVMAMGTRFK PENRPVRTSM HDDLVAGRRM
     EVDEVLGPLA AAAEQLQVPA PAFLSAYRVL KTLNSYL
//
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