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F0NQG4 (F0NQG4_SULIH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 15. 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:SiH_2095 EMBL ADX83439.1
OrganismSulfolobus islandicus (strain HVE10/4) [Complete proteome] [HAMAP]
Taxonomic identifier930943 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus ›

Protein attributes

Sequence length418 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

Region110 – 1112Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107
Region243 – 2464Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1371Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1401N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site3001Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
F0NQG4 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 818CE94F75A644F3

FASTA41846,575
        10         20         30         40         50         60 
MSKKVDELVK EDQEYLMQSF RRWYPFAIDR GSGAIVYDIE GKEYIDFNAG IGVVALGHKN 

        70         80         90        100        110        120 
EKIISAVKEQ MEKFFHYSLT DFYYEIAVEV AKRLSSLMPF SAKVFYTNSG TESVEAAIKI 

       130        140        150        160        170        180 
ARGHTRRQWI IGFLNSFHGR TLGSLAFTSS KAIQRKSFSP LLPSTYLIPY PDKRDPLCKE 

       190        200        210        220        230        240 
DCTEALLGFI EDWIFKKVVD PNEIAAFIAE PIQGEGGVIV PPKDFFYKLN NLLKKFGILL 

       250        260        270        280        290        300 
ILDEVQTGIG RTGKMFAFEH FNVTPDLVCL AKALGGGLPL GAVIGRKEIM DLPPGSHANT 

       310        320        330        340        350        360 
FGGNPLALAA AKVILEEVPK LLDHVSSIGK KIIEELKDTR SPYLYDVRGL GLLIGAELRK 

       370        380        390        400        410 
DNKPFVEGLE KVLYNSFRRG VLAIGAGESV VRIEPPLIIE EDLALKGTRI LIEEIEKL

« Hide

References

[1]"Genome analyses of icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host interaction studies."
Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S., Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q., Huang L., Garrett R.A.
J. Bacteriol. 193:1672-1680(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HVE10/4 EMBL ADX83439.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002426 Genomic DNA. Translation: ADX83439.1.
RefSeqYP_005646653.1. NC_017275.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX83439; ADX83439; SiH_2095.
GeneID12416214.
KEGGsih:SiH_2095.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00823.
OMAKIIEDAH.

Enzyme and pathway databases

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 nameF0NQG4_SULIH
AccessionPrimary (citable) accession number: F0NQG4
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 15 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