argD

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

Pathwayⁱ: L-arginine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

Arginine biosynthesis bifunctional protein ArgJ (argJ)
Acetylglutamate kinase (Deima_1346), Acetylglutamate/acetylaminoadipate kinase (argB)
N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate reductase (argC)
Acetylornithine/acetyl-lysine aminotransferase (argD), Acetylornithine/acetyl-lysine aminotransferase (argD)

This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayⁱ: L-lysine biosynthesis via AAA pathway

This protein is involved in step 4 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (Thermus route).UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:

no protein annotated in this organism
Acetylglutamate/acetylaminoadipate kinase (argB)
N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC)
Acetylornithine/acetyl-lysine aminotransferase (argD), Acetylornithine/acetyl-lysine aminotransferase (argD)
no protein annotated in this organism

This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (Thermus route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	Length	Description
Binding siteⁱ	160 – 160	1	Pyridoxal phosphate; via carbonyl oxygenUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107
Binding siteⁱ	163 – 163	1	N2-acetyl-L-ornithineUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107
Binding siteⁱ	326 – 326	1	N2-acetyl-L-ornithineUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107
Binding siteⁱ	327 – 327	1	Pyridoxal phosphateUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107

GO - Molecular functionⁱ

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

GO - Biological processⁱ

arginine biosynthetic process Source: UniProtKB-HAMAP
lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

Complete GO annotation...

Keywords - Molecular functionⁱ

AminotransferaseUniRule annotationSAAS annotationImported, Transferase

Keywords - Biological processⁱ

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

Keywords - Ligandⁱ

Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCycⁱ	DMAR709986:GHZG-2028-MONOMER.
UniPathwayⁱ	UPA00033; UER00038. UPA00068; UER00109.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acetylornithine/acetyl-lysine aminotransferaseUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107 (EC:2.6.1.11UniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107 ) Short name: ACOATUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107
Gene namesⁱ	Name:argDUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107 Synonyms:lysJUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107 Ordered Locus Names:Deima_1982Imported Automatic assertion inferred from database entriesⁱ EMBL:ADV67627.1
Organismⁱ	Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34)Imported Automatic assertion inferred from database entriesⁱ EMBL:ADV67627.1 Proteomes:UP000008635
Taxonomic identifierⁱ	709986 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus maricopensis
Proteomesⁱ	UP000008635 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01107

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

CytoplasmUniRule annotation

PTM / Processingⁱ

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Modified residueⁱ	299 – 299	1	N6-(pyridoxal phosphate)lysineUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGⁱ	709986.Deima_1982.

STRINGⁱ

709986.Deima_1982.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	E8U988.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	269 – 272	4	Pyridoxal phosphate bindingUniRule annotation Automatic assertion according to rulesⁱ HAMAP-Rule:MF_01107

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	ENOG4108JPW. Bacteria. COG0160. LUCA.
HOGENOMⁱ	HOG000020206.
KOⁱ	K00823.
OMAⁱ	HIPYGTH.
OrthoDBⁱ	POG091H0APS.

Family and domain databases

CDDⁱ	cd00610. OAT_like. 1 hit.
Gene3Dⁱ	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAPⁱ	MF_01107. ArgD_aminotrans_3. 1 hit.
InterProⁱ	IPR004636. AcOrn/SuccOrn_fam. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHERⁱ	PTHR11986. PTHR11986. 1 hit.
Pfamⁱ	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAMⁱ	SSF53383. SSF53383. 1 hit.
PROSITEⁱ	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

E8U988-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTATTARQPE LKTALPGPNT KAIMERDAKH LSTSYMRPYP FVPDRGEGVW 
        60         70         80         90        100
LTDVDGNTML DFFAGIAVST TGHAHPHVVQ AVQAQIERFA HVCLTDYPQE 
       110        120        130        140        150
ITTSLAERLV RHVERTLPDG RHEKWRVFLG NSGAEAVEAA VKLARNHTGR 
       160        170        180        190        200
SHIISTIGSF HGRTYGAITL TGSKTKYKRG FGPLLPNVSH VPYPNPFRPP 
       210        220        230        240        250
LGSTAETCGQ AVLNYLEDVL FQTVIPADEV AAIIVEPMQG EGGYIVPPAD 
       260        270        280        290        300
FLPGLRALCD RHGIMLIFDE VQAGMGRTGK MFSYQNFDGV QPDIITLAKG 
       310        320        330        340        350
IASGLPISAM MAKESVMTWP VGSHGSTFGG NPVAAAAAHA TLDLLEGAVK 
       360        370        380        390        400
HPGCGDNLMD NARTVGDYIL SELRDMQTEF PFLGDVRGQG LFIGLEFVKP 
       410        420        430        440        450
DGSPDGKLRD AASMAMFERG LLNLDCGESV IRISPPLILT REDAETGLNI 

MRETLRSLQ

Length:459

Mass (Da):49,701

Last modified:April 5, 2011 - v1

Checksum:ⁱ053F3D31E4A07A8C

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP002454 Genomic DNA. Translation: ADV67627.1.
RefSeqⁱ	WP_013557132.1. NC_014958.1.

Genome annotation databases

EnsemblBacteriaⁱ	ADV67627; ADV67627; Deima_1982.
KEGGⁱ	dmr:Deima_1982.
PATRICⁱ	46925045. VBIDeiMar159729_1991.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP002454 Genomic DNA. Translation: ADV67627.1.
RefSeqⁱ	WP_013557132.1. NC_014958.1.

3D structure databases

ProteinModelPortalⁱ	E8U988.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	709986.Deima_1982.

STRINGⁱ

709986.Deima_1982.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ADV67627; ADV67627; Deima_1982.
KEGGⁱ	dmr:Deima_1982.
PATRICⁱ	46925045. VBIDeiMar159729_1991.

Phylogenomic databases

eggNOGⁱ	ENOG4108JPW. Bacteria. COG0160. LUCA.
HOGENOMⁱ	HOG000020206.
KOⁱ	K00823.
OMAⁱ	HIPYGTH.
OrthoDBⁱ	POG091H0APS.

Enzyme and pathway databases

UniPathwayⁱ	UPA00033; UER00038. UPA00068; UER00109.
BioCycⁱ	DMAR709986:GHZG-2028-MONOMER.

Family and domain databases

CDDⁱ	cd00610. OAT_like. 1 hit.
Gene3Dⁱ	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAPⁱ	MF_01107. ArgD_aminotrans_3. 1 hit.
InterProⁱ	IPR004636. AcOrn/SuccOrn_fam. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHERⁱ	PTHR11986. PTHR11986. 1 hit.
Pfamⁱ	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAMⁱ	SSF53383. SSF53383. 1 hit.
PROSITEⁱ	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

E8U988_DEIML

Accessionⁱ

Primary (citable) accession number: E8U988

Entry historyⁱ

Integrated into UniProtKB/TrEMBL:	April 5, 2011
Last sequence update:	April 5, 2011
Last modified:	September 7, 2016
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteomeImported

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 one 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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - E8U988 (E8U988_DEIML)

UniProt

E8U988 - E8U988_DEIML

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Acetylornithine/acetyl-lysine aminotransferase

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/pathway' target='_top'>More...</a></p>Pathwayi: L-arginine biosynthesis

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via AAA pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Amino acid modifications

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Functionⁱ

Pathwayⁱ: L-arginine biosynthesis

Pathwayⁱ: L-lysine biosynthesis via AAA pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ