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Q9X2A5 (ARGD_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:TM_1785
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length385 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 – 385385Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112805

Regions

Region94 – 952Pyridoxal phosphate binding HAMAP MF_01107
Region211 – 2144Pyridoxal phosphate binding HAMAP MF_01107

Sites

Binding site1261Pyridoxal phosphate; via carbonyl oxygen
Binding site1291N2-acetyl-L-ornithine By similarity
Binding site2671N2-acetyl-L-ornithine By similarity
Binding site2681Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2401N6-(pyridoxal phosphate)lysine HAMAP MF_01107

Secondary structure

1 ................................................................ 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X2A5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4018F87FCBEBFFE0

FASTA38542,884
        10         20         30         40         50         60 
MYLMNTYSRF PATFVYGKGS WIYDEKGNAY LDFTSGIAVN VLGHSHPRLV EAIKDQAEKL 

        70         80         90        100        110        120 
IHCSNLFWNR PQMELAELLS KNTFGGKVFF ANTGTEANEA AIKIARKYGK KKSEKKYRIL 

       130        140        150        160        170        180 
SAHNSFHGRT LGSLTATGQP KYQKPFEPLV PGFEYFEFNN VEDLRRKMSE DVCAVFLEPI 

       190        200        210        220        230        240 
QGESGIVPAT KEFLEEARKL CDEYDALLVF DEVQCGMGRT GKLFAYQKYG VVPDVLTTAK 

       250        260        270        280        290        300 
GLGGGVPIGA VIVNERANVL EPGDHGTTFG GNPLACRAGV TVIKELTKEG FLEEVEEKGN 

       310        320        330        340        350        360 
YLMKKLQEMK EEYDVVADVR GMGLMIGIQF REEVSNREVA TKCFENKLLV VPAGNNTIRF 

       370        380 
LPPLTVEYGE IDLAVETLKK VLQGI

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of acetylornithine aminotransferase from Thermotoga maritima."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PLP.
[3]"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution."
Joint center for structural genomics (JCSG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PLP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD36848.1.
PIRD72211.
RefSeqNP_229582.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E54X-ray1.50A1-385[»]
2ORDX-ray1.40A/B1-385[»]
ProteinModelPortalQ9X2A5.
SMRQ9X2A5. Positions 1-385.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897842.
GenomeReviewsGene locus TM_1785 in contig AE000512_GR.
KEGGtma:TM1785.
NMPDRfig|243274.1.peg.1766.
PATRIC23938555. VBITheMar51294_1805.
TIGRTM_1785.

Phylogenomic databases

HOGENOMHBG725944.
OMAEHIDEMS.
PhylomeDBQ9X2A5.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycTMAR243274:TM_1785-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_THEMA
AccessionPrimary (citable) accession number: Q9X2A5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 91 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