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Oxidoreductase
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PDB id
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2cvo
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Contents |
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* Residue conservation analysis
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PDB id:
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Oxidoreductase
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Title:
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Crystal structure of putative n-acetyl-gamma-glutamyl- phosphate reductase (ak071544) from rice (oryza sativa)
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Structure:
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Putative semialdehyde dehydrogenase. Chain: a, b, c, d. Fragment: residues 50-415. Synonym: n-acetyl-gamma-glutamyl-phosphate reductase. Engineered: yes
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Source:
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Oryza sativa. Rice. Organism_taxid: 4530. Gene: ak071544. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Tetramer (from
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Resolution:
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2.20Å
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R-factor:
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0.171
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R-free:
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0.213
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Authors:
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T.Nonaka,A.Kita,J.Miura-Ohnuma,E.Katoh,N.Inagaki,T.Yamazaki, K.Miki
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Key ref:
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T.Nonaka
et al.
(2005).
Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa).
Proteins,
61,
1137-1140.
PubMed id:
DOI:
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Date:
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10-Jun-05
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Release date:
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06-Dec-05
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PROCHECK
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Headers
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References
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Q6AV34
(ARGC_ORYSJ) -
Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
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Seq:
Struc:
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415 a.a.
348 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.1.2.1.38
- N-acetyl-gamma-glutamyl-phosphate reductase.
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Pathway:
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Ornithine Biosynthesis
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Reaction:
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5- glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde
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+
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NADP(+)
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+
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phosphate
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=
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N-acetyl-5- glutamyl phosphate
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+
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NADPH
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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oxidation-reduction process
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4 terms
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Biochemical function
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nucleotide binding
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5 terms
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DOI no:
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Proteins
61:1137-1140
(2005)
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PubMed id:
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Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa).
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T.Nonaka,
A.Kita,
J.Miura-Ohnuma,
E.Katoh,
N.Inagaki,
T.Yamazaki,
K.Miki.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. Ribbon model of the overall structure of the OsAGPR
tetramer.
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Figure 2.
Figure 2. (A) Stereo view of the comparison of the C  models
of OsAGPR (red) and HiASADH complexed with NADP[19] (blue; PDB
ID: 1pqu) by stereo drawings of C -trace
models. The aspartate-  -semialdehyde
(green) covalently bonded to catalytic Cys136 and the phosphate
ion (orange) interacted with Arg172 taken from the complex
structure[20] (PDB ID: 1nx6) are also superimposed. (B) Stereo
view of the transparent superimposition of NADP (blue; PDB ID:
1pqu), covalently bonded aspartate- -semialdehyde
(ASA, green; PDB ID: 1nx6), and a phosphate ion (Pi; PDB ID:
1nx6) from the HiASADH complexes onto the putative active site
of OsAGPR (pale red). The catalytic site and mechanism are
thought to be similar between AGPRs and ASADHs. The flexible
side-chain of Arg279 has variable conformations between the
chain A-D of OsAGPR.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
61,
1137-1140)
copyright 2005.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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I.C.Chen,
W.D.Lin,
S.K.Hsu,
V.Thiruvengadam,
and
W.H.Hsu
(2009).
Isolation and characterization of a novel lysine racemase from a soil metagenomic library.
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Appl Environ Microbiol, 75,
5161-5166.
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F.Moradian,
C.Garen,
L.Cherney,
M.Cherney,
and
M.N.James
(2006).
Expression, purification, crystallization and preliminary X-ray analysis of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
986-988.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
