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Q2RG62 (ARGC_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:Moth_2290
OrganismMoorella thermoacetica (strain ATCC 39073)
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeMoorella groupMoorella

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 Probable 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
Reference 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_1000011019

Sites

Active site1501 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RG62 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 6C6EAED5BE084DB2

FASTA34637,549
        10         20         30         40         50         60 
MIKAGIIGAT GYTGAELVRI LSRHPEVELV ALTSRSYAGE GMAGVYPSLT GYTNLTCENL 

        70         80         90        100        110        120 
TPDEVMDRAE VIFIALPHGH AVPVATRARE RGIKVIDLGA DWRFRNARTY EEWYKIQHGN 

       130        140        150        160        170        180 
HELAARAVYG LPEIHREAIR SAGLVANPGC YPTSAILGLA PLLKGGYIDP ATIIIDAKSG 

       190        200        210        220        230        240 
VSGAGREARV TSLFVECNES INPYGVASHR HTPEIEQELS ALAGKEVKVT FTPHLLPISR 

       250        260        270        280        290        300 
GILSTMYATL VRPASTEELR RVYEKFYAGE PFVHLLPPGQ WPHTRWVYGS NNCHLNLAVD 

       310        320        330        340 
TRTGRVVVAS AIDNLTKGAS GQAVQNLNLM CGFPETMALE VPGLCP 

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed: 18631365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC20577.1.
RefSeqYP_431120.1. NC_007644.1.

3D structure databases

HSSPHSSP built from PDB template 1VKN based on UniProtKB Q9X2A2.
ProteinModelPortalQ2RG62.
SMRQ2RG62. Positions 1-346.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2RG62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3831322.
GenomeReviewsGene locus Moth_2290 in contig CP000232_GR.
KEGGmta:Moth_2290.
NMPDRfig|264732.9.peg.2327.
PATRIC22642052. VBIMooThe6753_2494.

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMATAEDCTT.
PhylomeDBQ2RG62.

Enzyme and pathway databases

BioCycMTHE264732:MOTH_2290-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_MOOTA
AccessionPrimary (citable) accession number: Q2RG62
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 48 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