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Q9RW75 (ARGD_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylornithine/acetyl-lysine aminotransferase
Short name=ACOAT
EC=2.6.1.-
EC=2.6.1.11
Gene names
Name:argD
Synonyms:lysJ
Ordered Locus Names:DR_0794
OrganismDeinococcus radiodurans
Taxonomic identifier1299 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_01107

Catalytic activity

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

N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate 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

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 4/5. HAMAP MF_01107

Subunit structure

Homodimer By similarity. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

Sequence similarities

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

Sequence caution

The sequence AAF10373.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Acetylornithine/acetyl-lysine aminotransferase HAMAP MF_01107
PRO_0000112742

Regions

Region112 – 1132Pyridoxal phosphate binding By similarity
Region226 – 2294Pyridoxal phosphate binding By similarity

Sites

Binding site1391Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1421N2-acetyl-L-ornithine By similarity
Binding site2831N2-acetyl-L-ornithine By similarity
Binding site2841Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2551N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RW75 [UniParc].

Last modified February 12, 2003. Version 2.
Checksum: BA614DEDBA7B1025

FASTA42946,613
        10         20         30         40         50         60 
MTGNEQNPSK WLAAEKKYDS GVYNKHDVVM VRGQGATVWD ENGRSYIDCV VGYGVATLGH 

        70         80         90        100        110        120 
SHPDVVKAVQ EQAGKLMVMP QTVPNDKRAE FLQELVGVLP QGLDRVFLCN SGTEAMEAAK 

       130        140        150        160        170        180 
KFAITATGRS RFVSMKRGFS GRSLGALSFT WEPKYREPFG DAVDNKSVDF VTYGNLDELR 

       190        200        210        220        230        240 
AAVTEQTAAV IMEPVQGEGG VRPASAEFIQ EARRITREKG ALLILDEIQT GFCRTGKMFA 

       250        260        270        280        290        300 
CEHFGVIPDG MTLAKAIAGG TPTAAFAMMS EVADRMPAGG HGTTFGGNPL SMAAGVASLR 

       310        320        330        340        350        360 
AMKREGLAEQ AREKGAYMMD KLRAIQSPKI REVRGLGLMI GVELKEKSAP YIHAMEHDEG 

       370        380        390        400        410        420 
VLCLAATPLV VRFLPPAVIS KEQIDQVVAA FERVLNNVNP REERQAELRA QQSEMGQQQV 


SQGESVQTE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF10373.1. Different initiation.
PIRE75474.
RefSeqNP_294518.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RW75.
SMRQ9RW75. Positions 12-395.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1798912.
GenomeReviewsGene locus DR_0794 in contig AE000513_GR.
KEGGdra:DR_0794.
NMPDRfig|243230.1.peg.977.
PATRIC21629136. VBIDeiRad64572_0974.
TIGRDR_0794.

Phylogenomic databases

HOGENOMHBG725944.
PhylomeDBQ9RW75.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycDRAD243230:DR_0794-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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_DEIRA
AccessionPrimary (citable) accession number: Q9RW75
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: January 25, 2012
This is version 83 of the entry and version 2 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

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