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E8U988 (E8U988_DEIML) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

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

Protein namesRecommended name:
Acetylornithine/acetyl-lysine aminotransferase HAMAP-Rule MF_01107
Short name=ACOAT HAMAP-Rule MF_01107
EC=2.6.1.- HAMAP-Rule MF_01107
EC=2.6.1.11 HAMAP-Rule MF_01107
Gene names
Name:argD HAMAP-Rule MF_01107
Synonyms:lysJ HAMAP-Rule MF_01107
Ordered Locus Names:Deima_1982 EMBL ADV67627.1
OrganismDeinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34) [Complete proteome] [HAMAP] EMBL ADV67627.1
Taxonomic identifier709986 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate. HAMAP-Rule MF_01107

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

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_01107

Pathway

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

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01107

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01107.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. HAMAP-Rule MF_01107

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region269 – 2724Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1601Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1631N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3261N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3271Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2991N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
E8U988 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 053F3D31E4A07A8C

FASTA45949,701
        10         20         30         40         50         60 
MTATTARQPE LKTALPGPNT KAIMERDAKH LSTSYMRPYP FVPDRGEGVW LTDVDGNTML 

        70         80         90        100        110        120 
DFFAGIAVST TGHAHPHVVQ AVQAQIERFA HVCLTDYPQE ITTSLAERLV RHVERTLPDG 

       130        140        150        160        170        180 
RHEKWRVFLG NSGAEAVEAA VKLARNHTGR SHIISTIGSF HGRTYGAITL TGSKTKYKRG 

       190        200        210        220        230        240 
FGPLLPNVSH VPYPNPFRPP LGSTAETCGQ AVLNYLEDVL FQTVIPADEV AAIIVEPMQG 

       250        260        270        280        290        300 
EGGYIVPPAD FLPGLRALCD RHGIMLIFDE VQAGMGRTGK MFSYQNFDGV QPDIITLAKG 

       310        320        330        340        350        360 
IASGLPISAM MAKESVMTWP VGSHGSTFGG NPVAAAAAHA TLDLLEGAVK HPGCGDNLMD 

       370        380        390        400        410        420 
NARTVGDYIL SELRDMQTEF PFLGDVRGQG LFIGLEFVKP DGSPDGKLRD AASMAMFERG 

       430        440        450 
LLNLDCGESV IRISPPLILT REDAETGLNI MRETLRSLQ

« Hide

References

[1]"The complete genome of Deinococcus maricopensis DSM 21211."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P. expand/collapse author list , Woyke T., Wu D., Pukall R., Gehrich-Schroeter G., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002454 Genomic DNA. Translation: ADV67627.1.
RefSeqYP_004171292.1. NC_014958.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV67627; ADV67627; Deima_1982.
GeneID10151337.
KEGGdmr:Deima_1982.
PATRIC46925045. VBIDeiMar159729_1991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000020206.
KOK00823.

Enzyme and pathway databases

BioCycDMAR709986:GHZG-2028-MONOMER.
UniPathwayUPA00033; UER00038.
UPA00068; UER00109.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_01107. ArgD_aminotrans_3.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR004636. Trfase_AcOrn/SuccOrn_fam.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 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 nameE8U988_DEIML
AccessionPrimary (citable) accession number: E8U988
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info