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Reviewed, UniProtKB/Swiss-Prot Q0B5P6 (ARGC_BURCM)

Last modified February 9, 2010. Version 31. 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: Bamb_4978
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length315 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_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 HAMAP MF_01110.

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 – 315315N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_01110
PRO_1000137114

Sites

Active site1171 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0B5P6-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5F921A6364279910

FASTA31533,429
        10         20         30         40         50         60 
MSLPIVYIDG DQGTTGLQIH ERLRDRTDLR LVTLPDAERK DPARRAEAIN ASDIAILCLP 

        70         80         90        100        110        120 
DAAAREAVGF IRNPAVRVID ASSAHRTEPD WVYGFPEMVD GHAQTIAHAR RVTNPGCYPT 

       130        140        150        160        170        180 
GAVGLLRPLQ QAGLLPRDYP VCIHAVSGYS GGGRAAVDAF ESNGAARAQP LQVYGLALAH 

       190        200        210        220        230        240 
KHVPEIQLHA GLAHRPLFVP AYGAYRQGIV LTVPIELRLL PAGVTGEALH ACLAHHYAGA 

       250        260        270        280        290        300 
RRVEVTPLAD TRAITHLDPQ ALNGSNDLRL SVFVNAEHGQ VLLAAVFDNL GKGASGAAVQ 

       310 
NLDLMLGVAS AVKAA 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000441 Genomic DNA. Translation: ABI90527.1.
RefSeqYP_776861.1.

3D structure databases

SMRQ0B5P6. Positions 6-310.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0B5P6.

Genome annotation databases

GeneID4313869.
GenomeReviewsGene locus Bamb_4978 in contig CP000441_GR.
KEGGbam:Bamb_4978.
NMPDRfig|339670.3.peg.1712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMAEIQQHAG.

Family and domain databases

HAMAPMF_01110. ArgC_type2.
[Tree]
InterProIPR010136. AGPR_subtype.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01851. argC_other. 1 hit.
PROSITEPS01224. ARGC. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGC_BURCM
AccessionPrimary (citable) accession number: Q0B5P6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 31 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