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Database: UniProt
Entry: A0A0G3XKK8_9SPHN
LinkDB: A0A0G3XKK8_9SPHN
Original site: A0A0G3XKK8_9SPHN 
ID   A0A0G3XKK8_9SPHN        Unreviewed;       337 AA.
AC   A0A0G3XKK8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AB433_17985 {ECO:0000313|EMBL:AKM12035.1};
OS   Croceicoccus naphthovorans.
OG   Plasmid p1 {ECO:0000313|EMBL:AKM12035.1,
OG   ECO:0000313|Proteomes:UP000035287}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM12035.1, ECO:0000313|Proteomes:UP000035287};
RN   [1] {ECO:0000313|EMBL:AKM12035.1, ECO:0000313|Proteomes:UP000035287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PQ-2 {ECO:0000313|EMBL:AKM12035.1,
RC   ECO:0000313|Proteomes:UP000035287};
RC   PLASMID=Plasmid p1 {ECO:0000313|Proteomes:UP000035287};
RA   Zeng Y., Huang Y.;
RL   Submitted (JUN-2015) 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; CP011771; AKM12035.1; -; Genomic_DNA.
DR   RefSeq; WP_007016014.1; NZ_JACIEL010000032.1.
DR   AlphaFoldDB; A0A0G3XKK8; -.
DR   KEGG; cna:AB433_17985; -.
DR   PATRIC; fig|1348774.3.peg.3786; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000035287; Plasmid p1.
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   Plasmid {ECO:0000313|EMBL:AKM12035.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035287}.
FT   DOMAIN          8..157
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;  36029 MW;  FF045C676D7C810E CRC64;
     MTKQLHFCIH GAGGLGSVVG GFLARRGHKV TLIARKPHVE AIRQGGLQIE GVRAQFVQRD
     NLFAVETPAE VEDAIDYYIL LTKAKGTDQA LADATVLVDR TACALTLQNG VGKEGRLQAA
     FGKDKVIGGS IMDGATLLEP GRALNNMAVP VTAYFGELGG GESDRTRTMA EALDSAGMGS
     RSTADITHVH WEKLVQVGSA SSWSASTLGG IKELDFIDGV AVREGAAQYV LIVKDLLAIY
     KALGYEPRNF FAPVSRLVEI NGQSFDEALA GVMAMVGRFK PENRPARTSM HDDLVAGRRM
     EVDEVLGPLA EAAERLGVDA PTFLGAYRVL KTLNSYL
//
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