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Q5HA98 (ARGC_EHRRW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:Erum7830, ERWE_CDS_08280
OrganismEhrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]
Taxonomic identifier254945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length347 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
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 – 347347N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_0000112405

Sites

Active site1521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HA98 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 2C694FE760B3C0A6

FASTA34738,870
        10         20         30         40         50         60 
MSYQVSVAVV GATGYVGVEL VRLLLFHPMV KIKYLCATQS IGSLLSSHYD HVLKDSIPVS 

        70         80         90        100        110        120 
ISCFSSIDLS KVDVIFLCLP HGQSNEIVKK IHNEVKIIID LSADFRIKDI DTYKEWYGAH 

       130        140        150        160        170        180 
CCPDLIQDFV YGLTEIYWEE IKKSRFVACP GCYATSALVP LFPLLRLRLV KSQNIIVDAK 

       190        200        210        220        230        240 
SGVSGAGRSV DQKKLFCEIH DVIKSYNISK HRHIPEIEQE LCFAACQENI NVQFVPNLIP 

       250        260        270        280        290        300 
VKRGMLSSIY LELEEGVSPI DIREALLVFY KDSKFIFIDE EKAITTKSVI GTNYCYIGVF 

       310        320        330        340 
PGRIPNTVII VCNIDNLLKG ASGQAVQNFN IMMSCDETTA LLNIPYL 

« Hide

References

[1]"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number."
Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. expand/collapse author list , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A.
Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed: 15637156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.
[2]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed: 16547041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Welgevonden.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR767821 Genomic DNA. Translation: CAH58517.1.
CR925678 Genomic DNA. Translation: CAI27322.1.
RefSeqYP_180646.1. NC_005295.2.
YP_197704.1. NC_006832.1.

3D structure databases

ProteinModelPortalQ5HA98.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HA98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3233272.
3261127.
GenomeReviewsGene locus Erum7830 in contig CR767821_GR.
Gene locus ERWE_CDS_08280 in contig CR925678_GR.
KEGGeru:Erum7830.
erw:ERWE_CDS_08280.
PATRIC20581548. VBIEhrRum92411_0878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMATAEDCTT.
PhylomeDBQ5HA98.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycERUM254945-1:ERUM7830-MONOMER.
ERUM254945:ERWE_CDS_08280-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_EHRRW
AccessionPrimary (citable) accession number: Q5HA98
Secondary accession number(s): Q5FDQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 57 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