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Database: UniProt
Entry: A8TJF1_9PROT
LinkDB: A8TJF1_9PROT
Original site: A8TJF1_9PROT 
ID   A8TJF1_9PROT            Unreviewed;       327 AA.
AC   A8TJF1;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 68.
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=BAL199_16873 {ECO:0000313|EMBL:EDP66754.1};
OS   alpha proteobacterium BAL199.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP66754.1, ECO:0000313|Proteomes:UP000003417};
RN   [1] {ECO:0000313|EMBL:EDP66754.1, ECO:0000313|Proteomes:UP000003417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL199 {ECO:0000313|EMBL:EDP66754.1,
RC   ECO:0000313|Proteomes:UP000003417};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-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}.
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:EDP66754.1}.
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DR   EMBL; ABHC01000001; EDP66754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8TJF1; -.
DR   STRING; 331869.BAL199_16873; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000003417; 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:SF42; 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   Reference proteome {ECO:0000313|Proteomes:UP000003417}.
FT   DOMAIN          3..171
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          198..318
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   327 AA;  34146 MW;  84A4ECF592D41A17 CRC64;
     MRIGIVGAGA VGGFLAGHLA RAGTEVALLA RGPHLAALRE RGLTVESQGQ RWTVQVPASD
     RASDLGEMDA VVVTAKAPAL PAIAAAIAPM LGPDTPVICA MNGIPWWYDH GRAGAAADRT
     IARLDPDGAI WRGIGPQRAI GCVVDCPAQV VEPGLVRHVA PRPGALTLGE PKGGTSERMT
     RLAAVIEASG MKAPMVDDIR AALWSKLFVN ISRSPLGVLT GATERELAAD PDTLSVTLAI
     MHEAQAVARA HGIEVAIDVE RQSNPQNRSE HRSSMLQDWD LGRPMEIDGI VRVVQDFARA
     AGVPTPTLDV VATLLVAKAR GAGIYAG
//
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