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UniProtKB/Swiss-Prot entry Q6NHH0

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

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Entry information
Entry name ARGC_CORDI
Primary accession number Q6NHH0
Secondary accession numbers None
Integrated into Swiss-Prot on August 30, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 34)
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: DIP1167
From
Corynebacterium diphtheriae [TaxID: 1717] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
DOI=10.1093/nar/gkg874; PubMed=14602910 [NCBI, ExPASy, EBI, Israel, Japan]
Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J.;
"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129.";
Nucleic Acids Res. 31:6516-6523(2003).
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
BX248357; CAE49687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_939524.1; -.
3D structure databases
ModBase Q6NHH0.
Enzyme and pathway databases
BioCyc CDIP257309:DIP1167-MON; -.
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: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.
BLOCKS Q6NHH0.
ProtoNet Q6NHH0.
Genome annotation databases
GeneID 2648567; -.
GenomeReviews BX248353_GR; DIP1167.
KEGG cdi:DIP1167; -.
NMPDR fig|257309.1.peg.1115; -.
Phylogenomic databases
HOGENOM Q6NHH0; -.
Genome annotation databases
CMR Q6NHH0; DIP1167.
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   347  347     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_0000112398
ACT_SITE   151   151        By similarity. 
Sequence information
Length: 347 AA [This is the length of the unprocessed precursor] Molecular weight: 36437 Da [This is the MW of the unprocessed precursor] CRC64: 7644E555E152AC5B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNIKVAIVGA SGYAGGEILR LLLQHPLYLS GQLSIGALMG SSTVGQTVSE LMPHLPELSD 

        70         80         90        100        110        120 
RVVEPTDVET LKSHDVVFLA LPHGFSAEIA QQLPAEITVI DCAADFRLKD QKDWDAYYGG 

       130        140        150        160        170        180 
KHAGSWPYGI PEMPGHRDLI ASSKRIAVPG CFPTGATLAL LPAIAAHIIE PDVSVVSITG 

       190        200        210        220        230        240 
VSGAGKKASV AMLGAETMGS LKAYNVAGKH RHTPEISQNL SEYADQKIVV SFTPVLAPLP 

       250        260        270        280        290        300 
RGILTTATAK LTSGITLDEI REIYLNAYEN EPFVHILPSG QQPQTQAVVG SNMCHIQVDA 

       310        320        330        340 
DDNSKKLVVT SAIDNLTKGT AGAAVQCMNL SLGVSETSGL PCGGVAP
Q6NHH0 in FASTA format

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