Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q59279 (ARGC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. 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:Cgl1394, cg1580
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

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.

Sequence caution

The sequence CAF21405.1 differs from that shown. Reason: Erroneous initiation.

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 – 347347N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_0000112400

Sites

Active site1511 By similarity

Experimental info

Sequence conflict141A → T in AAB62245. Ref.1
Sequence conflict141A → T in AAC24812. Ref.2
Sequence conflict211L → I in AAB62245. Ref.1
Sequence conflict211L → I in AAC24812. Ref.2
Sequence conflict251H → Q in AAB62245. Ref.1
Sequence conflict251H → Q in AAC24812. Ref.2
Sequence conflict1021C → R in AAB62245. Ref.1
Sequence conflict1021C → R in AAC24812. Ref.2
Sequence conflict2771L → S in AAB62245. Ref.1
Sequence conflict2771L → S in AAC24812. Ref.2
Sequence conflict3411P → A in AAB62245. Ref.1
Sequence conflict3411P → A in AAC24812. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q59279 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: 44A73448E7BF4864

FASTA34735,888
        10         20         30         40         50         60 
MTIKVAIAGA SGYAGGEILR LLLGHPAYAS GELEIGALTA ASTAGSTLGE LMPHIPQLAD 

        70         80         90        100        110        120 
RVIQDTTAET LAGHDVVFLG LPHGFSAEIA LQLGPDVTVI DCAADFRLQN AADWEKFYGS 

       130        140        150        160        170        180 
EHQGTWPYGI PEMPGHREAL RGAKRVAVPG CFPTGATLAL LPAVQAGLIE PDVSVVSITG 

       190        200        210        220        230        240 
VSGAGKKASV ALLGSETMGS LKAYNTSGKH RHTPEIAQNL GEVSDKPVKV SFTPVLAPLP 

       250        260        270        280        290        300 
RGILTTATAP LKEGVTAEQA RAVYEEFYAQ ETFVHVLPEG AQPQTQAVLG SNMCHVQVEI 

       310        320        330        340 
DEEAGKVLVT SAIDNLTKGT AGAAVQCMNL SVGFDEAAGL PQVGVAP 

« Hide

References

« Hide 'large scale' references
[1]Chun J.Y., Lee E.J., Cheon C.I., Min K.H., Lee M.-S.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]"Molecular cloning of the arginine biosynthetic genes from Corynebacterium glutamicum."
Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[3]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]"Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway."
Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N., Hallet J.-N., Glansdorff N.
Microbiology 142:99-108(1996) [PubMed: 8581175] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-347.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005242 Genomic DNA. Translation: AAB62245.1.
AF049897 Genomic DNA. Translation: AAC24812.1.
BA000036 Genomic DNA. Translation: BAB98787.1.
BX927152 Genomic DNA. Translation: CAF21405.1. Different initiation.
X86157 Genomic DNA. Translation: CAA60096.1.
RefSeqNP_600613.1. NC_003450.3.
YP_225681.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ59279.
SMRQ59279. Positions 4-347.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019370.
3344983.
GenomeReviewsGene locus Cgl1394 in contig BA000036_GR.
Gene locus cg1580 in contig BX927147_GR.
KEGGcgb:cg1580.
cgl:NCgl1340.
PATRIC21494827. VBICorGlu203724_1363.

Phylogenomic databases

HOGENOMHBG294213.
OMAVCRIAVH.
PhylomeDBQ59279.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycCGLU196627:CG1580-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_CORGL
AccessionPrimary (citable) accession number: Q59279
Secondary accession number(s): O32353
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2002
Last modified: January 25, 2012
This is version 87 of the entry and version 3 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