Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0JV20 (ARGC_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyl-gamma-glutamyl-phosphate reductase
Short name=AGPR
EC=1.2.1.38
Alternative name(s):
N-acetyl-glutamate semialdehyde dehydrogenase
Short name=NAGSA dehydrogenase
Gene names
Name:argC
Ordered Locus Names:Arth_1496
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP-Rule MF_00150

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP-Rule MF_00150

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity

Inferred from electronic annotation. Source: HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343N-acetyl-gamma-glutamyl-phosphate reductase HAMAP-Rule MF_00150
PRO_1000010975

Sites

Active site1461 By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JV20 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: E7CCF8508BE698BF

FASTA34334,930
        10         20         30         40         50         60 
MTISVAVSGA SGYAGGEVLR LLAGHPDVTI GAITAHSNAG SRLGELQPHL HGLASRILED 

        70         80         90        100        110        120 
TTVENLSGHD VVFLALPHGA SADIAAQLPE GTVVIDAGAD HRLEDPAAWE KFYGSAHAGT 

       130        140        150        160        170        180 
WPYGLPELPG QREKLKGANR IAVPGCYPTS ALLALTPGFA GSLLQPDDVV IVAASGTSGA 

       190        200        210        220        230        240 
GKAAKVNLIG SEVMGSMSPY GVGGGHRHTP EIEQGLGNAA GEAVTVSFTP TLAPMSRGIL 

       250        260        270        280        290        300 
TTATAKVKPG VTAAELRSAW EEAYDDEPFV HLLPEGQWPS TKSVQGSNHA VMQVAFDAHT 

       310        320        330        340 
GRVIVTCAID NLTKGTAGGA VQSMNIALGL AETAGLNLQG VAP

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000454 Genomic DNA. Translation: ABK02890.1.
RefSeqYP_830990.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JV20.
SMRA0JV20. Positions 3-343.
ModBaseSearch...

Protein-protein interaction databases

STRING290399.Arth_1496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK02890; ABK02890; Arth_1496.
GeneID4445992.
KEGGart:Arth_1496.
PATRIC20998289. VBIArtSp72239_1854.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHOG000254904.
KOK00145.
OMAVCRIAVH.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycASP290399:GHIF-1524-MONOMER.
UniPathwayUPA00068; UER00108.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00150. ArgC_type1.
InterProIPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
PfamPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01850. argC. 1 hit.
PROSITEPS01224. ARGC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGC_ARTS2
AccessionPrimary (citable) accession number: A0JV20
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents