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Q5HWN8 (ARGC_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:CJE0275
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length342 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 – 342342N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_0000112394

Sites

Active site1471 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HWN8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 80584471E19322D9

FASTA34238,886
        10         20         30         40         50         60 
MKIKVGILGA SGYAGNELVR ILLNHPKVEI SYLGSSSSVG QNYQDLYPNT PLNLCFENKN 

        70         80         90        100        110        120 
LDELELDLLF LATPHEFSAK LLNENLLKKM KIIDLSADFR LKNPKDYELW YKFTHPNQEL 

       130        140        150        160        170        180 
LQNAVYGLCE LYKEEIKKAS LVANPGCYTT CSILSLYPLF KEKIIDFSSV IIDAKSGVSG 

       190        200        210        220        230        240 
AGRSAKVENL FCEVNENIKA YNLALHRHTP EIEEHLSYAA KKKITLQFTP HLVSMQRGIL 

       250        260        270        280        290        300 
ISAYANLKED LQEQDIRDIY TKYYQNNKFI RLLPPQSLPQ TRWVKSSNFA DINFSVDQRT 

       310        320        330        340 
KRVIVLGAID NLIKGAAGQA VQNMNLMFDF DEDEGLKFFA NL 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW34867.1.
RefSeqYP_178297.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HWN8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HWN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3231037.
GenomeReviewsGene locus CJE0275 in contig CP000025_GR.
KEGGcjr:CJE0275.
PATRIC20042248. VBICamJej134361_0273.
TIGRCJE0275.

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMAVCRIAVH.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_0275-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_CAMJR
AccessionPrimary (citable) accession number: Q5HWN8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 54 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