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UniProtKB/Swiss-Prot entry A5VPX1

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

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Entry information
Entry name ARGC_BRUO2
Primary accession number A5VPX1
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on July 10, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 17)
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: BOV_0783
From
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [TaxID: 444178] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Brucella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Paulsen I.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000708; ABQ61374.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001258768.1; -.
3D structure databases
ModBase A5VPX1.
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: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_01110; -; 1.
PBIL [Tree]
InterPro IPR000706; AGPR_act_site.
IPR010136; AGPR_subtype.
IPR016040; NAD(P)-bd.
IPR000534; Semialdehyde_DHase_NAD-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01118; Semialdhyde_dh; 1.
Pfam graphical view of domain structure.
ProDom PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01851; argC_other; 1.
PROSITE PS01224; ARGC; 1.
BLOCKS A5VPX1.
ProtoNet A5VPX1.
Genome annotation databases
GeneID 5202374; -.
GenomeReviews CP000708_GR; BOV_0783.
KEGG bov:BOV_0783; -.
TIGR BOV_0783; -.
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   310  310     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_1000065140
ACT_SITE   117   117        By similarity. 
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 33744 Da [This is the MW of the unprocessed precursor] CRC64: 43274AC79823BF4F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKPKIFIDGE HGTTGLQIRT RLAERDDLEV ISIPEAERRN KDLRADYLRA ADIAILCLPD 

        70         80         90        100        110        120 
DASKEAVSLL EGHNSTRIID TSTAHRVHPD WAYGFAELAK GQRERIAEAR LVANPGCYPT 

       130        140        150        160        170        180 
GAIALVRPLC DAGLLPADYP VSVNAVSGYT GGGKQLIAQM EDRNHPDYLA ANNFLYGLPL 

       190        200        210        220        230        240 
KHKHVPELQL HGRLDRRPIF SPSVGRFPQG MIVQVPLFLS ELEGSPSLAK VHAVLTEHYA 

       250        260        270        280        290        300 
GQDIVEVVPL EESAKLPRVD AEELAGKDGM KLFVFGTEDH GQVNLVALLD NLGKGASGAA 

       310 
VQNMNLMLGK
A5VPX1 in FASTA format

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