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B0CD68 (ARGC_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:AM1_0609
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesAcaryochloris

Protein attributes

Sequence length352 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 By similarity 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 – 352352N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_1000076725

Sites

Active site1551 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CD68 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 179DFEF39CA1DE3E

FASTA35238,109
        10         20         30         40         50         60 
MGSQEDIPVG IIGASGYGGV QLTRLLLEHP HVHLAYLGGD SSAGRPFADL YPHLGFKQDL 

        70         80         90        100        110        120 
KVEAIDLDKV VERTQVVFLA LPNGLAAEMA PTLVECGCKV LDLSADYRFT NLDTYEDWYG 

       130        140        150        160        170        180 
TKRQDRDLAS TAVYGLPELY RQGISTASLV GCPGCFPTAS LLALAPLLKQ GLIDPNSAII 

       190        200        210        220        230        240 
DAKTGTSGGG RQAKTHLLLA EANGSIGPYG VAHHRHTPEI EQVSSDLAGR EVVVQFTPHL 

       250        260        270        280        290        300 
APMTRGILAT VYATMRDPGL VREDLITIFS AFYRNSPWVK VLPGSTYPFT KWAYGTNLCY 

       310        320        330        340        350 
LGIEVDQRTG RVIVISAIDN LMKGQAGQAV QCLNLMMGWP ETMGLPELTF YP 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW25659.1.
RefSeqYP_001514973.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CD68.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CD68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5679437.
GenomeReviewsGene locus AM1_0609 in contig CP000828_GR.
KEGGamr:AM1_0609.
PATRIC20615744. VBIAcaMar40141_0524.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG294213.
OMATAEDCTT.
PhylomeDBB0CD68.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycAMAR329726:AM1_0609-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_ACAM1
AccessionPrimary (citable) accession number: B0CD68
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 36 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