Skip Header

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

A5FPC2 (ARGC_DEHSB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:DehaBAV1_1371
OrganismDehalococcoides sp. (strain BAV1) [Complete proteome] [HAMAP]
Taxonomic identifier216389 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidetesDehalococcoides

Protein attributes

Sequence length341 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 – 341341N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150
PRO_1000118057

Sites

Active site1471 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FPC2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: BEE69BD1D191A885

FASTA34137,152
        10         20         30         40         50         60 
MKKYKAGIIN VTGYAGLELA RILESHPSVE LCSVTGRSLA GKKLSDVFPY LHRLDLPITE 

        70         80         90        100        110        120 
NLEGQVDVAF LALPHKEGAA LVPALLEKGM RVIDISADFR LKDPALYQAW YGFEHPCPGL 

       130        140        150        160        170        180 
LEEAVYGLPE LKRKDIAGAR LVANPGCYPT SAILGLVPAF KSDLIEPSAI IDAKSGLSGS 

       190        200        210        220        230        240 
GRTPTVKTIF CEADEDVCAY SIGTHRHQPE IAQELCRASG GVIPRVTFCP HLVPMSRGIL 

       250        260        270        280        290        300 
STAYARLKQP VTDEEVKEIY RQFYKDEPFV KVTAEPPHTR YTRGTNMCFI YPVVDALNEQ 

       310        320        330        340 
LIVISCIDNL VKGAAGQAVQ NMNIMLGLAE TEGLEAMATL P 

« Hide

References

[1]"Complete sequence of Dehalococcoides sp. BAV1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ritalahti K.M., Loeffler F., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BAV1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000688 Genomic DNA. Translation: ABQ17948.1.
RefSeqYP_001214826.1. NC_009455.1.

3D structure databases

ProteinModelPortalA5FPC2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FPC2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5131790.
GenomeReviewsGene locus DehaBAV1_1371 in contig CP000688_GR.
KEGGdeb:DehaBAV1_1371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0002.
HOGENOMHBG294213.
OMATAEDCTT.
ProtClustDBPRK00436.

Enzyme and pathway databases

BioCycDSP216389:DEHABAV1_1371-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_DEHSB
AccessionPrimary (citable) accession number: A5FPC2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 40 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