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A4YDF0 (A4YDF0_METS5) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 43. 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:Msed_0275
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera ›

Protein attributes

Sequence length417 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

Region109 – 1102Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107
Region242 – 2454Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1361Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1391N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2991Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2711N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
A4YDF0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 730C52FCAE8261AA

FASTA41745,922
        10         20         30         40         50         60 
MSLASRIIEE DSRYLMQSFS RWYPLVIERA KGSLVYDVDG KEYIDMNAGI GVMALGHGNE 

        70         80         90        100        110        120 
KIIRAVQEQM NKFFHYSLTD FYYDLAVRVA RKLVSLVGFQ GKVFYANSGT ESVEASLKIA 

       130        140        150        160        170        180 
RGHTGRQYII GFTNSFHGRT FGSMSFTSSK SVQRSAFSPL LPSTLLVPYP DRHNPLCRED 

       190        200        210        220        230        240 
CANAVLEYIE DWVLKKIVDP NDVAGFLLEP IQGEGGIIVP PREFLQGLQR IARKNGILLI 

       250        260        270        280        290        300 
LDEVQTGIGR TGKMFAFEHF GVEPDLICLA KALGGGLPLG AVVGRSEVMD LPRGSHANTF 

       310        320        330        340        350        360 
GGNALALAAA EVVLEEVPGL LGRVNSLGKM IVDILGSTKS RYVEEIRGMG LMIGVDLRRD 

       370        380        390        400        410 
GEPYEEGLEK VLRRSFERGV LAIGAGESVV RLLPPLVIEE ELAQRGSSII REEIDRL

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000682 Genomic DNA. Translation: ABP94452.1.
RefSeqYP_001190376.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YDF0.
ModBaseSearch...

Protein-protein interaction databases

STRING399549.Msed_0275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP94452; ABP94452; Msed_0275.
GeneID5103895.
KEGGmse:Msed_0275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
KOK00823.
OMAGGTGCQP.
ProtClustDBPRK05769.

Enzyme and pathway databases

BioCycMSED399549:GH1O-322-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 nameA4YDF0_METS5
AccessionPrimary (citable) accession number: A4YDF0
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 43 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