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Q9RVQ9 (ARGC1_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase
Short name=AGPR
EC=1.2.1.-
EC=1.2.1.38
Alternative name(s):
N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase
Short name=NAGSA dehydrogenase
Gene names
Name:argC1
Synonyms:lysY
Ordered Locus Names:DR_0963
OrganismDeinococcus radiodurans
Taxonomic identifier1299 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_00150

Catalytic activity

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP MF_00150

N(2)-acetyl-L-aminoadipate-semialdehyde + NADP+ + phosphate = N(2)-acetyl-L-gamma-aminoadipyl 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

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. HAMAP MF_00150

Subcellular location

Cytoplasm Probable HAMAP MF_00150.

Sequence similarities

Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Sequence caution

The sequence AAF10536.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

lysine 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150
PRO_0000112500

Sites

Active site1511 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RVQ9 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: 840EAEE18B423846

FASTA34837,775
        10         20         30         40         50         60 
MSTEKKTVAI VGGSGYAGGE FLRLALGHPH LEVTQVTSER SAKLPVSMVH PNLRGATNLK 

        70         80         90        100        110        120 
FRKAAELEEA DIIVLALPHN SAAKRITEFE AKGKVIVDLS ADFRLKDPEV YERFYGEPHP 

       130        140        150        160        170        180 
APEQLGQWVY GNPELHREDL RGATRIACAG CFATSVILAL YPLLRLGALA PKDIIATGLV 

       190        200        210        220        230        240 
GSSAAGASAS ESSHHPERAG SLRVYKPVGH RHTAEAQQEL PGKFPLHLTA ISTPRVRGIL 

       250        260        270        280        290        300 
TTIQAWVPDG WSDKDVWSAY REVYGQEPFI RIVKVAKGIH RYPDPMLLDG TNFCDIGFEM 

       310        320        330        340 
DVDTGRVVLM SAIDNLVKGT AGHAIQSLNV AQGWDERAGL GFLGLHPT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF10536.1. Different initiation.
PIRB75455.
RefSeqNP_294687.2. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RVQ9.
SMRQ9RVQ9. Positions 5-347.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1798963.
GenomeReviewsGene locus DR_0963 in contig AE000513_GR.
KEGGdra:DR_0963.
NMPDRfig|243230.1.peg.1146.
PATRIC21629496. VBIDeiRad64572_1150.
TIGRDR_0963.

Phylogenomic databases

HOGENOMHBG294213.
OMAVYRYPEP.
PhylomeDBQ9RVQ9.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycDRAD243230:DR_0963-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.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00145.
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 nameARGC1_DEIRA
AccessionPrimary (citable) accession number: Q9RVQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: January 25, 2012
This is version 92 of the entry and version 2 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

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