(data stored in SCRATCH zone)

SWISSPROT: E6S844_INTC7

ID   E6S844_INTC7            Unreviewed;       292 AA.
AC   E6S844;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   13-FEB-2019, entry version 47.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   OrderedLocusNames=Intca_0399 {ECO:0000313|EMBL:ADU46948.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46948.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46948.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate
CC       into pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.169;
CC         Evidence={ECO:0000256|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|RuleBase:RU362068}.
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DR   EMBL; CP002343; ADU46948.1; -; Genomic_DNA.
DR   RefSeq; WP_013491269.1; NC_014830.1.
DR   STRING; 710696.Intca_0399; -.
DR   EnsemblBacteria; ADU46948; ADU46948; Intca_0399.
DR   KEGG; ica:Intca_0399; -.
DR   eggNOG; ENOG4108KF8; Bacteria.
DR   eggNOG; COG1893; LUCA.
DR   HOGENOM; HOG000050222; -.
DR   KO; K00077; -.
DR   OrthoDB; 427052at2; -.
DR   BioCyc; ICAL710696:GH9U-408-MONOMER; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000008914; Chromosome.
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; 1.10.1040.10; -; 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   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00745; apbA_panE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6S844.
DR   SWISS-2DPAGE; E6S844.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
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:UP000008914}.
FT   DOMAIN        4    138       ApbA. {ECO:0000259|Pfam:PF02558}.
FT   DOMAIN      176    269       ApbA_C. {ECO:0000259|Pfam:PF08546}.
SQ   SEQUENCE   292 AA;  29548 MW;  945BD45CB055CAAE CRC64;
     MTRIGVLGPG GVGGVMAARL ARAGGDVVVV AGERTAAAIA AGGLHYTGPE GTWDGFVEAR
     SLLVAPVDVL IVATKAMDLA AALQRVPASL LGGSVVVPLL NGVDHLPYLR AELPGAQVVA
     SSVSVEATRH RPGVVEQVSG FCDVGVSVVN AEGHGWAQLA EEAGCTVTTA PDDATVLWRK
     LSFLAPLALL TTAAAAPIGP ALRRQPQLVR PIVAEAAAAA EAFGVTIDPD GIEERLRSLP
     ETMQSSMLKD LLGGRAVELD AIAGPVIRAL GHEGAPATVA AATEILARQG AT
//

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