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Protein

Acetylornithine/acetyl-lysine aminotransferase

Gene

argD

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in both the arginine and lysine biosynthetic pathways.UniRule annotation

Catalytic activityi

N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate semialdehyde + L-glutamate.UniRule annotation
N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotationNote: Binds 1 pyridoxal phosphate per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361Pyridoxal phosphate; via carbonyl oxygenUniRule annotation
Binding sitei139 – 1391N2-acetyl-L-ornithineUniRule annotation
Binding sitei299 – 2991Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
  2. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

AminotransferaseUniRule annotationImported, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesisUniRule annotation, Lysine biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciMSED399549:GH1O-289-MONOMER.
UniPathwayiUPA00033; UER00038.
UPA00068; UER00109.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylornithine/acetyl-lysine aminotransferaseUniRule annotation (EC:2.6.1.11UniRule annotation)
Short name:
ACOATUniRule annotation
Gene namesi
Name:argDUniRule annotation
Synonyms:lysJUniRule annotation
Ordered Locus Names:Msed_0275Imported
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)Imported
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
ProteomesiUP000000242 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi399549.Msed_0275.

Structurei

3D structure databases

ProteinModelPortaliA4YDF0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1102Pyridoxal phosphate bindingUniRule annotation
Regioni242 – 2454Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020206.
KOiK00823.
OMAiTDWFLFC.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4YDF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLASRIIEE DSRYLMQSFS RWYPLVIERA KGSLVYDVDG KEYIDMNAGI
60 70 80 90 100
GVMALGHGNE KIIRAVQEQM NKFFHYSLTD FYYDLAVRVA RKLVSLVGFQ
110 120 130 140 150
GKVFYANSGT ESVEASLKIA RGHTGRQYII GFTNSFHGRT FGSMSFTSSK
160 170 180 190 200
SVQRSAFSPL LPSTLLVPYP DRHNPLCRED CANAVLEYIE DWVLKKIVDP
210 220 230 240 250
NDVAGFLLEP IQGEGGIIVP PREFLQGLQR IARKNGILLI LDEVQTGIGR
260 270 280 290 300
TGKMFAFEHF GVEPDLICLA KALGGGLPLG AVVGRSEVMD LPRGSHANTF
310 320 330 340 350
GGNALALAAA EVVLEEVPGL LGRVNSLGKM IVDILGSTKS RYVEEIRGMG
360 370 380 390 400
LMIGVDLRRD GEPYEEGLEK VLRRSFERGV LAIGAGESVV RLLPPLVIEE
410
ELAQRGSSII REEIDRL
Length:417
Mass (Da):45,922
Last modified:May 28, 2007 - v1
Checksum:i730C52FCAE8261AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP94452.1.
RefSeqiWP_011921420.1. NC_009440.1.
YP_001190376.1. NC_009440.1.

Genome annotation databases

EnsemblBacteriaiABP94452; ABP94452; Msed_0275.
GeneIDi5103895.
KEGGimse:Msed_0275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP94452.1.
RefSeqiWP_011921420.1. NC_009440.1.
YP_001190376.1. NC_009440.1.

3D structure databases

ProteinModelPortaliA4YDF0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399549.Msed_0275.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP94452; ABP94452; Msed_0275.
GeneIDi5103895.
KEGGimse:Msed_0275.

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020206.
KOiK00823.
OMAiTDWFLFC.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00038.
UPA00068; UER00109.
BioCyciMSED399549:GH1O-289-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51363 / DSM 5348Imported.

Entry informationi

Entry nameiA4YDF0_METS5
AccessioniPrimary (citable) accession number: A4YDF0
Entry historyi
Integrated into UniProtKB/TrEMBL: May 28, 2007
Last sequence update: May 28, 2007
Last modified: March 31, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.