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Q9V1I6 (ARGC_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. 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:argC
Synonyms:lysY
Ordered Locus Names:PYRAB04410
ORF Names:PAB0291
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length330 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete 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 – 330330N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150
PRO_0000112492

Sites

Active site1421 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V1I6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CECC9E2AC23D4C8F

FASTA33036,962
        10         20         30         40         50         60 
MIKAAIVGGS GYIGGELIRL LSMHPEVEIT TITSRKFAGK KVHKVHPNLR GLNLRFTDKY 

        70         80         90        100        110        120 
EFDADVIFLA VPHGTSMRII GEFLGSAKII DLSADFRVSK DLYEKYYGSH EKPELIDKFV 

       130        140        150        160        170        180 
YGLPELHRKE IKRAELVANP GCNATAVILA LYPFRDVTSE AIVDLKVSSS AGGRRENVAS 

       190        200        210        220        230        240 
IHPERSHVVR VYKPFHHRHE AEVLQETGVK AMFTVHSVDI VRGLLATTYF KFEGSEKDLL 

       250        260        270        280        290        300 
KRLLMYRGEP FIRLVTDKGG LQRYPDPKYV IGSNFVDIGF SYDSENSRAI VFSALDNLIK 

       310        320        330 
GGAGQAVQNM NIMFGFDETL GLNYYPLYPG 

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49363.1.
PIRD75160.
RefSeqNP_126132.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V1I6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000003226; EBPYRP00000003157; EBPYRG00000003226.
GeneID1495336.
GenomeReviewsGene locus PYRAB04410 in contig AL096836_GR.
KEGGpab:PAB0291.
NMPDRfig|272844.1.peg.460.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022773.
HOGENOMHBG294213.
OMAVYRYPEP.
PhylomeDBQ9V1I6.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycPABY272844:PAB0291-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 nameARGC_PYRAB
AccessionPrimary (citable) accession number: Q9V1I6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 88 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