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UniProtKB/Swiss-Prot entry P59306

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARGC_ECOL6
Primary accession number P59306
Secondary accession numbers None
Integrated into Swiss-Prot on February 12, 2003
Sequence was last modified on February 12, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name N-acetyl-gamma-glutamyl-phosphate reductase
Synonyms AGPR
EC 1.2.1.38
N-acetyl-glutamate semialdehyde dehydrogenase
NAGSA dehydrogenase
Gene name
Name: argC
OrderedLocusNames: c4917
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014075; AAN83345.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_756771.1; -.
3D structure databases
SMR P59306; 1-334.
ModBase P59306.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003942; Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00150; -; 1.
PBIL [Tree]
InterPro IPR000706; AGPR_act_site.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
ProDom PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01850; argC; 1.
PROSITE PS01224; ARGC; 1.
ProtoNet P59306.
Genome annotation databases
GeneID 1040073; -.
GenomeReviews AE014075_GR; c4917.
KEGG ecc:c4917; -.
Phylogenomic databases
HOGENOM P59306; -.
Genome annotation databases
CMR P59306; c4917.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   334  334     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_0000112402
ACT_SITE   154   154        By similarity. 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 35946 Da [This is the MW of the unprocessed precursor] CRC64: B9CFCB23293F7B6D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLNTLIVGAS GYAGAELVTY VNRHPHMNIT ALTVSAQSND AGKLISDLHP QLKGIVDLPL 

        70         80         90        100        110        120 
QPMSDISEFS PGVDVVFLAT AHEVSHDLAP QFLEAGCVVF DLSGAFRVND VAFYEKYYGF 

       130        140        150        160        170        180 
THQYPELLEQ AAYGLAEWCG NKLKEANLIA VPGCYPTAAQ LALKPLIDAD LLDLNQWPVI 

       190        200        210        220        230        240 
NATSGVSGAG RKAAISNSFC EVSLQPYGVF THRHQPEIAT HLGADVIFTP HLGNFPRGIL 

       250        260        270        280        290        300 
ETITCRLKPG VSQVQVAQAL QQAYAHKPLV RLYDKGVPAL KNVVGLPFCD IGFAVQGEHL 

       310        320        330 
IIVATEDNLL KGAAAQAVQC ANIRFGYAET QSLI
P59306 in FASTA format

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