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Protein

Acetylornithine aminotransferase

Gene

argD

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 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'-phosphateNote: Binds 1 pyridoxal phosphate per subunit.

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), Acetylglutamate kinase (Tmari_1793)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine aminotransferase (argD), 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 sitei126 – 1261Pyridoxal phosphate; via carbonyl oxygen
Binding sitei129 – 1291N2-acetyl-L-ornithineBy similarity
Binding sitei267 – 2671N2-acetyl-L-ornithineBy similarity
Binding sitei268 – 2681Pyridoxal 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

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:TM_1785
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 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 – 385385Acetylornithine aminotransferasePRO_0000112805Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi243274.TM1785.

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 197Combined sources
Beta strandi21 – 244Combined sources
Beta strandi29 – 346Combined sources
Helixi35 – 384Combined sources
Helixi47 – 5913Combined sources
Beta strandi67 – 693Combined sources
Helixi70 – 8112Combined sources
Turni82 – 843Combined sources
Beta strandi87 – 937Combined sources
Helixi94 – 11219Combined sources
Beta strandi118 – 1236Combined sources
Helixi131 – 1366Combined sources
Helixi140 – 1434Combined sources
Helixi144 – 1463Combined sources
Beta strandi153 – 1564Combined sources
Helixi161 – 1677Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi179 – 1813Combined sources
Turni183 – 1853Combined sources
Helixi191 – 20414Combined sources
Beta strandi207 – 2115Combined sources
Turni213 – 2208Combined sources
Beta strandi221 – 2244Combined sources
Helixi225 – 2295Combined sources
Beta strandi234 – 2385Combined sources
Helixi240 – 2434Combined sources
Beta strandi249 – 2535Combined sources
Turni255 – 2573Combined sources
Helixi273 – 28614Combined sources
Helixi291 – 31222Combined sources
Beta strandi316 – 3227Combined sources
Beta strandi325 – 3306Combined sources
Helixi336 – 34510Combined sources
Beta strandi351 – 3533Combined sources
Turni354 – 3563Combined sources
Beta strandi357 – 3604Combined sources
Helixi368 – 38316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E54X-ray1.50A1-385[»]
2ORDX-ray1.40A/B1-385[»]
ProteinModelPortaliQ9X2A5.
SMRiQ9X2A5. Positions 1-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2A5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 952Pyridoxal phosphate binding
Regioni211 – 2144Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
InParanoidiQ9X2A5.
KOiK00821.
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.

Q9X2A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLMNTYSRF PATFVYGKGS WIYDEKGNAY LDFTSGIAVN VLGHSHPRLV
60 70 80 90 100
EAIKDQAEKL IHCSNLFWNR PQMELAELLS KNTFGGKVFF ANTGTEANEA
110 120 130 140 150
AIKIARKYGK KKSEKKYRIL SAHNSFHGRT LGSLTATGQP KYQKPFEPLV
160 170 180 190 200
PGFEYFEFNN VEDLRRKMSE DVCAVFLEPI QGESGIVPAT KEFLEEARKL
210 220 230 240 250
CDEYDALLVF DEVQCGMGRT GKLFAYQKYG VVPDVLTTAK GLGGGVPIGA
260 270 280 290 300
VIVNERANVL EPGDHGTTFG GNPLACRAGV TVIKELTKEG FLEEVEEKGN
310 320 330 340 350
YLMKKLQEMK EEYDVVADVR GMGLMIGIQF REEVSNREVA TKCFENKLLV
360 370 380
VPAGNNTIRF LPPLTVEYGE IDLAVETLKK VLQGI
Length:385
Mass (Da):42,884
Last modified:November 1, 1999 - v1
Checksum:i4018F87FCBEBFFE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36848.1.
PIRiD72211.
RefSeqiNP_229582.1. NC_000853.1.
WP_004082331.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36848; AAD36848; TM_1785.
GeneIDi897842.
KEGGitma:TM1785.
PATRICi23938555. VBITheMar51294_1805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36848.1.
PIRiD72211.
RefSeqiNP_229582.1. NC_000853.1.
WP_004082331.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E54X-ray1.50A1-385[»]
2ORDX-ray1.40A/B1-385[»]
ProteinModelPortaliQ9X2A5.
SMRiQ9X2A5. Positions 1-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36848; AAD36848; TM_1785.
GeneIDi897842.
KEGGitma:TM1785.
PATRICi23938555. VBITheMar51294_1805.

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
InParanoidiQ9X2A5.
KOiK00821.
OMAiTGKMWGY.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00109.

Miscellaneous databases

EvolutionaryTraceiQ9X2A5.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Crystal structure of acetylornithine aminotransferase from Thermotoga maritima."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PLP.
  3. "Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution."
    Joint center for structural genomics (JCSG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PLP.

Entry informationi

Entry nameiARGD_THEMA
AccessioniPrimary (citable) accession number: Q9X2A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 13, 2016
This is version 126 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.