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P63567 (ARGD_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylornithine aminotransferase

Short name=ACOAT
EC=2.6.1.11
Gene names
Name:argD
Ordered Locus Names:BR0301, BS1330_I0302
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length403 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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112733

Regions

Region219 – 2224Pyridoxal phosphate binding By similarity

Sites

Binding site1341Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1371N2-acetyl-L-ornithine By similarity
Binding site2761N2-acetyl-L-ornithine By similarity
Binding site2771Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63567 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: F413C19CD940A271

FASTA40343,453
        10         20         30         40         50         60 
MTDATTVHPL YDTYNRAALR FERGEGIWLI TEDGERYIDF AAGIAVNSLG HSHPHLVETL 

        70         80         90        100        110        120 
KTQAEKLWHL SNVYEIPAQE KLGRRLVEST FADKVFFTNS GAEALECAIK TARRYQYVSG 

       130        140        150        160        170        180 
HPERFRIITF EGAFHGRTLA TIAAGGQAKY LEGFGPKVEG FDQVPFGDEA ALRAAITPET 

       190        200        210        220        230        240 
AGILLEPIQG EGGLRAFPEE FLRLVRQICD ENGLLLLLDE VQTGVGRTGK LFAHEWAGIR 

       250        260        270        280        290        300 
PDIMAIAKGI GGGFPIGACL ATAEAAKGMT AGMHGTTYGG NPLGMAVGNA VLDVVLADGF 

       310        320        330        340        350        360 
MENVQATALV MKQGLASLVD RYPNVVSEIR GRGLLMGLKC VVPNTSLIQA LRDEHILSVG 

       370        380        390        400 
AGDNVVRLLP PLITTPEEAR EALKHIETAV ERLSIANPIS KTV 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29250.1.
CP002997 Genomic DNA. Translation: AEM17663.1.
RefSeqNP_697335.1. NC_004310.3.

3D structure databases

ProteinModelPortalP63567.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1165962.
GenomeReviewsGene locus BR0301 in contig AE014291_GR.
KEGGbms:BR0301.
PATRIC17788891. VBIBruSui107850_0314.
TIGRBR0301.

Phylogenomic databases

HOGENOMHBG725944.
OMAGRKLWHI.
PhylomeDBP63567.
ProtClustDBPRK01278.

Enzyme and pathway databases

BioCycBSUI204722:BR_0301-MONOMER.

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.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00821.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00707. ArgD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_BRUSU
AccessionPrimary (citable) accession number: P63567
Secondary accession number(s): G0K657, Q8YFA1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella suis

Brucella suis (strain 1330): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families