Skip Header

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

O66442 (ARGD_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylornithine aminotransferase
Short name=ACOAT
EC=2.6.1.11
Gene names
Name:argD
Ordered Locus Names:aq_023
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Pathway

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

Subunit structure

Homodimer Probable.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112715

Regions

Region96 – 972Pyridoxal phosphate binding HAMAP MF_01107
Region213 – 2164Pyridoxal phosphate binding By similarity

Sites

Binding site1281Pyridoxal phosphate; via carbonyl oxygen
Binding site1311N2-acetyl-L-ornithine By similarity
Binding site2701N2-acetyl-L-ornithine By similarity
Binding site2711Pyridoxal phosphate

Amino acid modifications

Modified residue2421N6-(pyridoxal phosphate)lysine HAMAP MF_01107

Secondary structure

1 ............................................................... 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66442 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: D4A963D54634030A

FASTA37642,009
        10         20         30         40         50         60 
MTYLMNNYAR LPVKFVRGKG VYLYDEEGKE YLDFVSGIGV NSLGHAYPKL TEALKEQVEK 

        70         80         90        100        110        120 
LLHVSNLYEN PWQEELAHKL VKHFWTEGKV FFANSGTESV EAAIKLARKY WRDKGKNKWK 

       130        140        150        160        170        180 
FISFENSFHG RTYGSLSATG QPKFHKGFEP LVPGFSYAKL NDIDSVYKLL DEETAGIIIE 

       190        200        210        220        230        240 
VIQGEGGVNE ASEDFLSKLQ EICKEKDVLL IIDEVQTGIG RTGEFYAYQH FNLKPDVIAL 

       250        260        270        280        290        300 
AKGLGGGVPI GAILAREEVA QSFTPGSHGS TFGGNPLACR AGTVVVDEVE KLLPHVREVG 

       310        320        330        340        350        360 
NYFKEKLKEL GKGKVKGRGL MLGLELEREC KDYVLKALEK GLLINCTAGK VLRFLPPLII 

       370 
QKEHIDRAIS VLREIL

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus vf5."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-376 IN COMPLEX WITH PLP.
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06390.1.
PIRG70301.
RefSeqNP_213001.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EH6X-ray1.90A/B2-376[»]
ProteinModelPortalO66442.
SMRO66442. Positions 2-376.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192639.
GenomeReviewsGene locus aq_023 in contig AE000657_GR.
KEGGaae:aq_023.
NMPDRfig|224324.1.peg.16.
PATRIC20957751. VBIAquAeo85532_0016.

Phylogenomic databases

HOGENOMHBG725944.
OMAVNEASED.
PhylomeDBO66442.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycAAEO224324:AQ_023-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.
KOK00818.
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_AQUAE
AccessionPrimary (citable) accession number: O66442
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 88 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents