Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A0B466 (ARGC_BURCH)

Last modified November 3, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bcen2424_5709
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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_01110

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP MF_01110

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the NAGSA dehydrogenase family. Type 2 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

oxidation reduction

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: HAMAP

NAD or NADH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_01110
PRO_1000137112

Sites

Active site1171 By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B466-1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: CC8CF751C341BA62

FASTA31333,216
        10         20         30         40         50         60 
MSFPTVFIDG DQGTTGLQIH ARLRDRTDVR LLTLPAAERK EAARRADALN ACDIAILCLP 

        70         80         90        100        110        120 
DAAAREAVGF IRNPAVRVID ASSAHRTQPD WVYGFPEMAD GHAHEIAHAK RVTNPGCYPT 

       130        140        150        160        170        180 
GAIGLLRPLL QAGLLPRDYP VSIHAVSGYS GGGRAAVDAF ESGDAAARAL PLQVYGLALA 

       190        200        210        220        230        240 
HKHVPEIRQH AGLAHRPFFV PAYGAYRQGI VLTIPIELRL LPAGVTGERL HACLAHHYAD 

       250        260        270        280        290        300 
ARHVDVMPLA DARAATHLDP QALNGTNDLR LGVFVNANGG QVLLSAVFDN LGKGASGAAV 

       310 
QNLDLMLGAR HAA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000459 Genomic DNA. Translation: ABK12442.1.
RefSeqYP_839335.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0B466.

Genome annotation databases

GeneID4452433.
GenomeReviewsGene locus Bcen2424_5709 in contig CP000459_GR.
KEGGbch:Bcen2424_5709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMA0B466.
OMAEIQQHAG.

Family and domain databases

HAMAPMF_01110.
[Tree]
InterProIPR000706. AGPR_act_site.
IPR010136. AGPR_subtype.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
ProDomPD003765. AGPR_act_site. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01851. argC_other. 1 hit.
PROSITEPS01224. ARGC. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGC_BURCH
AccessionPrimary (citable) accession number: A0B466
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 28, 2006
Last modified: November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents