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A5CSI9 (ARGC_CLAM3) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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

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:CMM_2001
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP]
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length349 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 MF_00150

Pathway

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

Subcellular location

Cytoplasm Probable HAMAP MF_00150.

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN-acetyl-gamma-glutamyl-phosphate reductase activity

Inferred from electronic annotation. Source: EC

NAD binding

Inferred from electronic annotation. Source: InterPro

protein dimerization activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_1000010988

Sites

Active site1521 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CSI9 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 4D8717CAD0CD8BF9

FASTA34936,032
        10         20         30         40         50         60 
MSFSVAVAGA SGYAGGELLR LLADHPRLEV QTLTAFQNAG ERLRQVHPHL TSYADRTFVE 

        70         80         90        100        110        120 
TTAERLAGHD VVFLALPHGK SGAITAELDD QTLVVDCGAD HRLVDEAAWD AFYGGDFAGA 

       130        140        150        160        170        180 
WPYGLPELLH AEEGGTQRTR LSGVKRIAVP GCNVTAITLG LQPGIRAGVI EPEDIVAVLA 

       190        200        210        220        230        240 
VGPSGAGRSL RTNLLASEIL GSASAYAVGG THRHTPEIRQ NLETAGGGHV SVSFTPVLVP 

       250        260        270        280        290        300 
MARGILATAT ARLAPGFSAH DVRAAWELAY ADEPFVHLLP EGSFPNVSDV TGSNTALVGL 

       310        320        330        340 
AIDEAAGRVV TVTAIDNLVK GTAGAAIQSA NIALGLPEAM GLPVNGVAP 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCPPB 382.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM711867 Genomic DNA. Translation: CAN02064.1.
RefSeqYP_001222743.1. NC_009480.1.

3D structure databases

ProteinModelPortalA5CSI9.
SMRA5CSI9. Positions 4-349.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5CSI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5175474.
GenomeReviewsGene locus CMM_2001 in contig AM711867_GR.
KEGGcmi:CMM_2001.
PATRIC21454831. VBIClaMic82482_2121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMAVCRIAVH.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycCMIC443906:CMM_2001-MONOMER.

Family and domain databases

HAMAPMF_00150. ArgC_type1.
[Tree]
InterProIPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00145.
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_CLAM3
AccessionPrimary (citable) accession number: A5CSI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 40 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