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UniProtKB/Swiss-Prot entry Q8KA61

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

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Entry information
Entry name ARGC_BUCAP
Primary accession number Q8KA61
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 48)
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: BUsg_045
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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
AE013218; AAM67616.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660405.1; -.
3D structure databases
ModBase Q8KA61.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG045-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: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 Q8KA61.
Genome annotation databases
GeneID 1005861; -.
GenomeReviews AE013218_GR; BUsg_045.
KEGG bas:BUsg045; -.
Phylogenomic databases
HOGENOM Q8KA61; -.
Genome annotation databases
CMR Q8KA61; BUsg_045.
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_0000112392
ACT_SITE   154   154        By similarity. 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 37835 Da [This is the MW of the unprocessed precursor] CRC64: 9F7487A9B3816B77 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLNVLIVGAS GYSGAELVNY INRHMFSKIK KIFVSENSSH IGKLFSELHQ EFKNIIDLPF 

        70         80         90        100        110        120 
EAINYDTLIE KDIDAVFLAT DHHVSYSLVP FFLSLNCVVF DLSGAYRVKN TDTYLKYYGF 

       130        140        150        160        170        180 
SHQHQDILKR SVYGLAEWNK QEIKKAELIA VPGCYATCIQ LALKPLIKEN FLNDEFIPII 

       190        200        210        220        230        240 
NAISGVSGAG RKANITNSFC EVSLHPYNVF THRHTPEIIE HLGIPVIFIP HLGSFSRGIL 

       250        260        270        280        290        300 
ASITCKLKCN FTFQDIYNLY NTVYKEKPLI RVYEKNFPSI KAVVKLPFCD IGFIIQDKYI 

       310        320        330 
VIIAAEDNLL KGAAAQAIQC FNIRFGFSEI ESII
Q8KA61 in FASTA format

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