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Protein

Acetylornithine aminotransferase

Gene

argD

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.

Cofactori

pyridoxal 5'-phosphateBy similarityNote: Binds 1 pyridoxal phosphate per subunit.By similarity

Pathwayi: L-arginine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Arginine biosynthesis bifunctional protein ArgJ (argJ), Arginine biosynthesis bifunctional protein ArgJ (argJ)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291Pyridoxal phosphate; via carbonyl oxygenBy similarity
Binding sitei132 – 1321N2-acetyl-L-ornithineBy similarity
Binding sitei271 – 2711N2-acetyl-L-ornithineBy similarity
Binding sitei272 – 2721Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-3772-MONOMER.
UniPathwayiUPA00068; UER00109.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylornithine aminotransferase (EC:2.6.1.11)
Short name:
ACOAT
Gene namesi
Name:argD
Ordered Locus Names:MSMEG_3773, MSMEI_3684
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Acetylornithine aminotransferasePRO_0000396816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431N6-(pyridoxal phosphate)lysineBy similarity
Cross-linki304 – 304Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi246196.MSMEG_3773.

Structurei

3D structure databases

ProteinModelPortaliA0QYS9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni214 – 2174Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
KOiK00818.
OMAiTGKMWGY.
OrthoDBiEOG6QVRHN.

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.
TIGRFAMsiTIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0QYS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLQSRWEAV MMNNYGTPPL SLVSGEGAVV TDADGREYLD LLGGIAVNLL
60 70 80 90 100
GHRHPAVIEA VTTQLDTLGH TSNLYATEPG IALAEALVGQ LGTQARVFFC
110 120 130 140 150
NSGTEANEVA FKITRLTGKT KIVAAEGAFH GRTMGSLALT GQPSKQAPFE
160 170 180 190 200
PLPGNVMHVP YGDVAALEAA VDDQTAAVFL EPIMGEGGVV VPPAGYLVAA
210 220 230 240 250
REITSKHGAL LVLDEVQTGV GRTGAFFAHQ HDGIVPDVVT MAKGLGGGLP
260 270 280 290 300
IGACLAVGAT GDLLTPGLHG STFGGNPVCT AAGLAVLKTL AAEDLVARAG
310 320 330 340 350
VLGKTLSHGI EELGHPLVDK VRGKGLLQGI VLTVPSAKAV ETAARDAGFL
360 370 380 390
VNAAAPEVVR LAPPLIITEG QIEAFITALP AVLDTAAEDS
Length:390
Mass (Da):39,796
Last modified:January 9, 2007 - v1
Checksum:i51D702618A820F13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75110.1.
CP001663 Genomic DNA. Translation: AFP40143.1.
RefSeqiWP_011729315.1. NZ_CP009494.1.
YP_888067.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK75110; ABK75110; MSMEG_3773.
AFP40143; AFP40143; MSMEI_3684.
GeneIDi4531216.
KEGGimsb:LJ00_18745.
msg:MSMEI_3684.
msm:MSMEG_3773.
PATRICi18079939. VBIMycSme59918_3712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK75110.1.
CP001663 Genomic DNA. Translation: AFP40143.1.
RefSeqiWP_011729315.1. NZ_CP009494.1.
YP_888067.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QYS9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_3773.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK75110; ABK75110; MSMEG_3773.
AFP40143; AFP40143; MSMEI_3684.
GeneIDi4531216.
KEGGimsb:LJ00_18745.
msg:MSMEI_3684.
msm:MSMEG_3773.
PATRICi18079939. VBIMycSme59918_3712.

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
KOiK00818.
OMAiTGKMWGY.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00109.
BioCyciMSME246196:GJ4Y-3772-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.
TIGRFAMsiTIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: PUPYLATION AT LYS-304, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiARGD_MYCS2
AccessioniPrimary (citable) accession number: A0QYS9
Secondary accession number(s): I7FN58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: November 11, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.