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CATH domain | Related DB codes (homologues) |
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1.10.1040.10 : N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2 | D00007,D00012,T00002,T00227 | 3.40.50.720 : Rossmann fold | S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109 |
KEGG pathways | MAP code | Pathways |
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MAP00770 | Pantothenate and CoA biosynthesis |
UniProtKB:Accession Number | P0A9J4 | Q604L6 | B5RXG4 | Q46RB9 | Q39SB2 | O34661 | Q99R37 | Q831Q5 | Q7MT04 |
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Entry name | PANE_ECOLI | Q604L6_METCA | B5RXG4_RALSO | Q46RB9_CUPPJ | Q39SB2_GEOMG | PANE_BACSU | Q99R37_STAAM | Q831Q5_ENTFA | Q7MT04_PORGI |
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Activity | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. |
| (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. | (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. |
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Subunit | Monomer. |
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Subcellular location | Cytoplasm (Potential). |
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Cofactor |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[1] | Scheme 2, p.16248-16251 |
| [2] | p.14499 |
| [3] | Scheme 9, p.704-708 |
| [4] | Fig.7, p.8935-3937 |
| [6] | Scheme 2, p.8495-8496 |
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references | [1] |
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PubMed ID | 11123955 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 16244-51 |
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Authors | Zheng R, Blanchard JS |
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Title | Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue. |
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[2] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), PROTEIN SEQUENCE OF 1-9, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. |
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PubMed ID | 11724562 |
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Journal | Biochemistry |
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Year | 2001 |
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Volume | 40 |
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Pages | 14493-500 |
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Authors | Matak-Vinkovi? D, Vinkovi? M, Saldanha SA, Ashurst JL, von Delft F, Inoue T, Miguel RN, Smith AG, Blundell TL, Abell C |
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Title | Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism. |
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Related PDB | 1ks9 |
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Related UniProtKB | P0A9J4 |
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[3] |
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PubMed ID | 15565250 |
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Journal | Nat Prod Rep |
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Year | 2004 |
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Volume | 21 |
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Pages | 695-721 |
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Authors | Webb ME, Smith AG, Abell C |
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Title | Biosynthesis of pantothenate. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH NADP. |
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PubMed ID | 15966718 |
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Journal | Biochemistry |
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Year | 2005 |
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Volume | 44 |
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Pages | 8930-9 |
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Authors | Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL |
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Title | The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. |
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Related PDB | 1yjq |
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Related UniProtKB | P0A9J4 |
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[5] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP ANALOG, MUTAGENESIS OF ASN-98; LYS-176 AND GLU-256. |
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PubMed ID | 17242510 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 2007 |
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Volume | 63 |
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Pages | 171-8 |
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Authors | Ciulli A, Lobley CM, Tuck KL, Smith AG, Blundell TL, Abell C |
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Title | pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study. |
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Related PDB | 1yon |
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Related UniProtKB | P0A9J4 |
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[6] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-72 AND SER-244. |
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PubMed ID | 17229734 |
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Journal | J Biol Chem |
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Year | 2007 |
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Volume | 282 |
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Pages | 8487-97 |
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Authors | Ciulli A, Chirgadze DY, Smith AG, Blundell TL, Abell C |
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Title | Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity. |
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Related PDB | 2ofp |
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Related UniProtKB | P0A9J4 |
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comments | According to the literature [6], this enzyme catalyzes the following reaction: (0) The sidechain of Glu256 and the amide groups of both sidechain and mainchain of Asn98 may modulate the activity of nicotinamide group through ribose hydroxyl groups. Moreover, the sidechain of Asn98 might modulate the activity of Lys176 as well as the substrate through its carboxyl group. (1) The pro-S hydride of NADPH transfers to the si-face of substrate, 2-dehydropantoate (or ketopantoate). At the same time, Lys176 acts as a general acid to protonate the C2 carbonyl oxygen during the developing C2-alkoxide.
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created | updated |
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2010-03-23 | 2012-02-24 |
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