ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5HWN8

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ARGC_CAMJR
Primary accession number Q5HWN8
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 30)
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: CJE0275
From
Campylobacter jejuni (strain RM1221) [TaxID: 195099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0030015; PubMed=15660156 [NCBI, ExPASy, EBI, Israel, Japan]
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
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
CP000025; AAW34867.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_178297.1; -.
3D structure databases
ModBase Q5HWN8.
Enzyme and pathway databases
BioCyc CJEJ195099:CJE_0275-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 Q5HWN8.
Genome annotation databases
GeneID 3231037; -.
GenomeReviews CP000025_GR; CJE0275.
KEGG cjr:CJE0275; -.
TIGR CJE0275; -.
Phylogenomic databases
HOGENOM Q5HWN8; -.
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   342  342     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_0000112394
ACT_SITE   147   147        By similarity. 
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 38886 Da [This is the MW of the unprocessed precursor] CRC64: 80584471E19322D9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKIKVGILGA SGYAGNELVR ILLNHPKVEI SYLGSSSSVG QNYQDLYPNT PLNLCFENKN 

        70         80         90        100        110        120 
LDELELDLLF LATPHEFSAK LLNENLLKKM KIIDLSADFR LKNPKDYELW YKFTHPNQEL 

       130        140        150        160        170        180 
LQNAVYGLCE LYKEEIKKAS LVANPGCYTT CSILSLYPLF KEKIIDFSSV IIDAKSGVSG 

       190        200        210        220        230        240 
AGRSAKVENL FCEVNENIKA YNLALHRHTP EIEEHLSYAA KKKITLQFTP HLVSMQRGIL 

       250        260        270        280        290        300 
ISAYANLKED LQEQDIRDIY TKYYQNNKFI RLLPPQSLPQ TRWVKSSNFA DINFSVDQRT 

       310        320        330        340 
KRVIVLGAID NLIKGAAGQA VQNMNLMFDF DEDEGLKFFA NL
Q5HWN8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!