Skip Header

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

A5GAY8 (ARGC_GEOUR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Gura_1051
OrganismGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]
Taxonomic identifier351605 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length346 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 By similarity 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 – 346346N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_1000076733

Sites

Active site1491 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GAY8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 44A5CBD26F4E3199

FASTA34637,492
        10         20         30         40         50         60 
MLKVAIVGAS GYTGVELLRL LHCHPEVAIT CVTSEQSAGK AISEVFPTLR SRYNLVLENL 

        70         80         90        100        110        120 
EPVRIADRAD FIFTALPHKA AMEVVPTFLK LGKRVVDLSA DYRLRDAKEY EAWYEPHMNP 

       130        140        150        160        170        180 
TLLEQSVYGL PELRREKIAG ADLVANPGCY PTSVILGLAP LLKKKLIDPA TIIADSKSGV 

       190        200        210        220        230        240 
SGAGRSAKVD NLYCEVNDGF KAYGVGGAHR HIPEIEQELS LLAGKQLKIS FTPHLVPMDR 

       250        260        270        280        290        300 
GILSTIYATP TGAVSSAELL ELYRAYYQGE AFVRILPEGS FPSTSHVRGS NFCDIGLAVD 

       310        320        330        340 
NRTGRVVVVS AIDNLIKGAS GQAVQNMNIM NGFPENLGLE ALALFP 

« Hide

References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
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., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rf4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000698 Genomic DNA. Translation: ABQ25257.1.
RefSeqYP_001229830.1. NC_009483.1.

3D structure databases

ProteinModelPortalA5GAY8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5GAY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5165881.
GenomeReviewsGene locus Gura_1051 in contig CP000698_GR.
KEGGgur:Gura_1051.
NMPDRfig|351605.3.peg.2264.
PATRIC22032066. VBIGeoUra13052_1126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMATAEDCTT.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycGURA351605:GURA_1051-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_GEOUR
AccessionPrimary (citable) accession number: A5GAY8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 43 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