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Reviewed, UniProtKB/Swiss-Prot Q8XWN8 (ARGD_RALSO)

Last modified January 19, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
Gene names
Name: argD
Ordered Locus Names: RSc2435
ORF Names: RS02668
OrganismRalstonia solanacearum (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107

Subunit structure

Homodimer By similarity. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112772

Regions

Region223 – 2264Pyridoxal phosphate binding By similarity

Sites

Binding site1381Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1411N(2)-acetyl-L-ornithine By similarity
Binding site2801Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XWN8-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: D1D6C190E8351FAC

FASTA39942,778
        10         20         30         40         50         60 
MAFADYPVQS LMYITNRPEI VFTEGKGSWL TDHNGKRYLD FVQGWAVNCL GHSNDGMIEA 

        70         80         90        100        110        120 
LNAQAKKLIN PSPAFYNEPM AKLAGLLSAH SCFDKVFFAN SGAEANEGAI KLARKWGKKH 

       130        140        150        160        170        180 
KSGAGKNRFE IITFDHSFHG RTLATMSASG KAGWDTIFAP QVPGFPKAIL NDIASVEALI 

       190        200        210        220        230        240 
TDETVGVMLE PVQGEGGVLP ATQEFMQQLR ALTRKHKLLL IVDEVQAGCG RCGTLFAYQL 

       250        260        270        280        290        300 
SNIEPDIMTL GKGIGGGVPL SALLCTDEVA SFEAGDQGGT YNGNPLMTAV GCSVIEQLLA 

       310        320        330        340        350        360 
PGFLAGVQER GAYLRAQLLE LSEAFGLAGE RGEGLLRALL LGKDIGGQLV EAAREMNPTG 

       370        380        390 
LLLNAPRPNI LRFMPALNVT TDEIDTMIGM LRTLLKAHG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646052 Genomic DNA. Translation: CAD16142.1.
RefSeqNP_520556.1.

3D structure databases

SMRQ8XWN8. Positions 18-395.
ModBaseSearch...

Genome annotation databases

GeneID1221282.
GenomeReviewsGene locus RSc2435 in contig AL646052_GR.
KEGGrso:RSc2435.
NMPDRfig|267608.1.peg.2435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG725944.
OMALFAYELS.

Enzyme and pathway databases

BioCycRSOL267608:RSC2435-MONOMER.
BRENDA2.6.1.11. 97066.

Family and domain databases

HAMAPMF_01107. ArgD_aminotrans_3.
[Tree]
InterProIPR004636. AcOrn/succinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_RALSO
AccessionPrimary (citable) accession number: Q8XWN8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: March 1, 2002
Last modified: January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents