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Protein

Acetylornithine/succinyldiaminopimelate aminotransferase

Gene

argD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in both the arginine and lysine biosynthetic pathways.UniRule annotation1 Publication

Catalytic activityi

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.UniRule annotation1 Publication
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphate1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.1 Publication

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 annotation1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Amino-acid acetyltransferase (argA)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine/succinyldiaminopimelate 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 DAP pathway

This protein is involved in step 2 of the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route).UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (dapD)
  2. Acetylornithine/succinyldiaminopimelate aminotransferase (argD)
  3. Succinyl-diaminopimelate desuccinylase (dapE)
This subpathway is part of the pathway L-lysine biosynthesis via DAP 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 LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route), the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Pyridoxal phosphate; via carbonyl oxygenUniRule annotation
Binding sitei144 – 1441N2-acetyl-L-ornithineUniRule annotation
Binding sitei283 – 2831N2-acetyl-L-ornithineUniRule annotation
Binding sitei284 – 2841Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • arginine biosynthetic process via ornithine Source: EcoCyc
  • lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ACETYLORNTRANSAM-MONOMER.
ECOL316407:JW3322-MONOMER.
MetaCyc:ACETYLORNTRANSAM-MONOMER.
UniPathwayiUPA00034; UER00020.
UPA00068; UER00109.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylornithine/succinyldiaminopimelate aminotransferaseUniRule annotation (EC:2.6.1.11UniRule annotation, EC:2.6.1.17UniRule annotation)
Short name:
ACOATUniRule annotation
Short name:
DapATaseUniRule annotation
Short name:
Succinyldiaminopimelate transferaseUniRule annotation
Gene namesi
Name:argDUniRule annotation
Synonyms:dapCUniRule annotation, dtu
Ordered Locus Names:b3359, JW3322
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10066. argD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 406405Acetylornithine/succinyldiaminopimelate aminotransferasePRO_0000112743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei255 – 2551N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

EPDiP18335.
PaxDbiP18335.
PRIDEiP18335.

2D gel databases

SWISS-2DPAGEP18335.

Interactioni

Subunit structurei

Homodimer.Curated

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4260742. 7 interactions.
DIPiDIP-9138N.
IntActiP18335. 6 interactions.
STRINGi511145.b3359.

Structurei

3D structure databases

ProteinModelPortaliP18335.
SMRiP18335. Positions 16-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1092Pyridoxal phosphate bindingUniRule annotation
Regioni226 – 2294Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
InParanoidiP18335.
KOiK00821.
OMAiGHLFAYM.
OrthoDBiEOG6QVRHN.
PhylomeDBiP18335.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR017652. Ac/SucOrn_transaminase_bac.
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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18335-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG
60 70 80 90 100
IAVTALGHCH PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE
110 120 130 140 150
RVVFMNSGTE ANETAFKLAR HYACVRHSPF KTKIIAFHNA FHGRSLFTVS
160 170 180 190 200
VGGQPKYSDG FGPKPADIIH VPFNDLHAVK AVMDDHTCAV VVEPIQGEGG
210 220 230 240 250
VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA YMHYGVTPDI
260 270 280 290 300
LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD
310 320 330 340 350
IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY
360 370 380 390 400
KGRARDFLYA GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV

AKVVGA
Length:406
Mass (Da):43,767
Last modified:January 23, 2007 - v4
Checksum:i645AA1EBCA442214
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2473GVT → ALA in AAA23480 (PubMed:2199330).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32796 Genomic DNA. Translation: AAA23480.1.
U18997 Genomic DNA. Translation: AAA58156.1.
U00096 Genomic DNA. Translation: AAC76384.1.
AP009048 Genomic DNA. Translation: BAE77931.1.
PIRiB65130.
RefSeqiNP_417818.1. NC_000913.3.
WP_000963792.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76384; AAC76384; b3359.
BAE77931; BAE77931; BAE77931.
GeneIDi947864.
KEGGiecj:JW3322.
eco:b3359.
PATRICi32122152. VBIEscCol129921_3453.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32796 Genomic DNA. Translation: AAA23480.1.
U18997 Genomic DNA. Translation: AAA58156.1.
U00096 Genomic DNA. Translation: AAC76384.1.
AP009048 Genomic DNA. Translation: BAE77931.1.
PIRiB65130.
RefSeqiNP_417818.1. NC_000913.3.
WP_000963792.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP18335.
SMRiP18335. Positions 16-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260742. 7 interactions.
DIPiDIP-9138N.
IntActiP18335. 6 interactions.
STRINGi511145.b3359.

2D gel databases

SWISS-2DPAGEP18335.

Proteomic databases

EPDiP18335.
PaxDbiP18335.
PRIDEiP18335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76384; AAC76384; b3359.
BAE77931; BAE77931; BAE77931.
GeneIDi947864.
KEGGiecj:JW3322.
eco:b3359.
PATRICi32122152. VBIEscCol129921_3453.

Organism-specific databases

EchoBASEiEB0064.
EcoGeneiEG10066. argD.

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
InParanoidiP18335.
KOiK00821.
OMAiGHLFAYM.
OrthoDBiEOG6QVRHN.
PhylomeDBiP18335.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00020.
UPA00068; UER00109.
BioCyciEcoCyc:ACETYLORNTRANSAM-MONOMER.
ECOL316407:JW3322-MONOMER.
MetaCyc:ACETYLORNTRANSAM-MONOMER.

Miscellaneous databases

PROiP18335.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01107. ArgD_aminotrans_3.
InterProiIPR017652. Ac/SucOrn_transaminase_bac.
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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase."
    Heimberg H., Boyen A., Crabeel M., Glansdorff N.
    Gene 90:69-78(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  5. "The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis."
    Ledwidge R., Blanchard J.S.
    Biochemistry 38:3019-3024(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27 AND 69-77, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.

Entry informationi

Entry nameiARGD_ECOLI
AccessioniPrimary (citable) accession number: P18335
Secondary accession number(s): Q2M725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.