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Q4UVI5 (ARGC_XANC8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. 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:XC_1875
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length316 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 – 316316N-acetyl-gamma-glutamyl-phosphate reductase HAMAP-Rule MF_00150
PRO_1000011082

Sites

Active site1361 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4UVI5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 15C298DB06CE56C3

FASTA31634,263
        10         20         30         40         50         60 
MTVQPTTIGI VGARGHTGAE LIKLIAAHPQ LQLVFVSSRE LAGQRVAEHS DGYEGELRYE 

        70         80         90        100        110        120 
SLDADAVAAK AADVVILALP NGKAEPFVAA IDANRPQTLL IDLSADYRFD PAWYYGLPEL 

       130        140        150        160        170        180 
TRHTYAGQRR ISNPGCYATA MQLAITPLRE QLAGPPQCFG VSGYSGAGTT PSDKNNPALL 

       190        200        210        220        230        240 
ADNLMPYALT NHMHEREVSA QLGVPVEFMP HVAPHFRGIT MTVNLWLQQP LTREQIHARY 

       250        260        270        280        290        300 
LERYAHEPLI EIVDEAPWVS RIAGTQGVQI GGFTMAPGNK RVVVVATLDN LLKGAATQAM 

       310 
QNLNLALGWD ELTAIG 

« Hide

References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8004.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000050 Genomic DNA. Translation: AAY48938.1.
RefSeqYP_242958.1. NC_007086.1.

3D structure databases

HSSPHSSP built from PDB template 1VKN based on UniProtKB Q9X2A2.
ProteinModelPortalQ4UVI5.
ModBaseSearch...

Protein-protein interaction databases

STRING314565.XC_1875.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY48938; AAY48938; XC_1875.
GeneID3380422.
KEGGxcb:XC_1875.
PATRIC24065231. VBIXanCam24967_2014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHOG000254904.
KOK00145.
OMAVCRIAVH.
ProtClustDBPRK00436.

Enzyme and pathway databases

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.
[Graphical view]
PfamPF01118. Semialdhyde_dh. 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_XANC8
AccessionPrimary (citable) accession number: Q4UVI5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2005
Last modified: May 1, 2013
This is version 62 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