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Protein

Acetylornithine/acetyl-lysine aminotransferase

Gene

argD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in both the arginine and lysine biosynthetic pathways.By similarity

Catalytic activityi

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
N(2)-acetyl-L-lysine + 2-oxoglutarate = N-acetyl-L-aminoadipate 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)
  2. Acetylglutamate kinase (TTHA1903), Acetylglutamate/acetylaminoadipate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC)
  4. 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).
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Alpha-aminoadipate--LysW ligase LysX (lysX)
  2. Acetylglutamate/acetylaminoadipate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC), N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase (argC)
  4. Acetylornithine/acetyl-lysine aminotransferase (argD), Acetylornithine/acetyl-lysine aminotransferase (argD)
  5. N-acetyl-lysine deacetylase (lysK)
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401Pyridoxal phosphate; via carbonyl oxygenBy similarity
Binding sitei143 – 1431N2-acetyl-L-ornithine
Binding sitei282 – 2821N2-acetyl-L-ornithine
Binding sitei283 – 2831Pyridoxal phosphate

GO - Molecular functioni

GO - Biological processi

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

BioCyciTTHE300852:GH8R-1797-MONOMER.
UniPathwayiUPA00033; UER00038.
UPA00068; UER00109.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylornithine/acetyl-lysine aminotransferase (EC:2.6.1.-, EC:2.6.1.11)
Short name:
ACOAT
Gene namesi
Name:argD
Synonyms:lysJ
Ordered Locus Names:TTHA1755
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 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 – 395395Acetylornithine/acetyl-lysine aminotransferasePRO_0000311262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei254 – 2541N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi300852.TTHA1755.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Beta strandi31 – 366Combined sources
Beta strandi38 – 414Combined sources
Beta strandi46 – 516Combined sources
Helixi52 – 554Combined sources
Helixi64 – 7613Combined sources
Helixi87 – 9812Combined sources
Beta strandi104 – 1129Combined sources
Helixi113 – 12816Combined sources
Beta strandi132 – 1365Combined sources
Helixi145 – 1495Combined sources
Helixi154 – 1574Combined sources
Helixi158 – 1603Combined sources
Beta strandi167 – 1704Combined sources
Helixi175 – 1817Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi193 – 1953Combined sources
Turni196 – 1994Combined sources
Beta strandi200 – 2023Combined sources
Helixi205 – 21814Combined sources
Beta strandi221 – 2255Combined sources
Turni227 – 2348Combined sources
Beta strandi235 – 2384Combined sources
Helixi240 – 2434Combined sources
Beta strandi248 – 2525Combined sources
Helixi254 – 2574Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2735Combined sources
Helixi288 – 30417Combined sources
Helixi307 – 32216Combined sources
Beta strandi329 – 3357Combined sources
Beta strandi338 – 3458Combined sources
Helixi348 – 35811Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi369 – 3724Combined sources
Helixi380 – 39415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VEFX-ray1.35A/B1-395[»]
1WKGX-ray2.25A/B1-395[»]
1WKHX-ray2.25A/B1-395[»]
ProteinModelPortaliQ5SHH5.
SMRiQ5SHH5. Positions 9-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHH5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1142Pyridoxal phosphate binding
Regioni225 – 2284Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
KOiK05830.
OMAiFSEIRGM.
PhylomeDBiQ5SHH5.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3. 1 hit.
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.

Q5SHH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METRTLEDWR ALLEAEKTLD SGVYNKHDLL IVRGQGARVW DAEGNEYIDC
60 70 80 90 100
VGGYGVANLG HGNPEVVEAV KRQAETLMAM PQTLPTPMRG EFYRTLTAIL
110 120 130 140 150
PPELNRVFPV NSGTEANEAA LKFARAHTGR KKFVAAMRGF SGRTMGSLSV
160 170 180 190 200
TWEPKYREPF LPLVEPVEFI PYNDVEALKR AVDEETAAVI LEPVQGEGGV
210 220 230 240 250
RPATPEFLRA AREITQEKGA LLILDEIQTG MGRTGKRFAF EHFGIVPDIL
260 270 280 290 300
TLAKALGGGV PLGAAVMREE VARSMPKGGH GTTFGGNPLA MAAGVAAIRY
310 320 330 340 350
LERTRLWERA AELGPWFMEK LRAIPSPKIR EVRGMGLMVG LELKEKAAPY
360 370 380 390
IARLEKEHRV LALQAGPTVI RFLPPLVIEK EDLERVVEAV RAVLA
Length:395
Mass (Da):43,423
Last modified:December 21, 2004 - v1
Checksum:i1D3B73EAC3454C3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71578.1.
RefSeqiWP_011228893.1. NC_006461.1.
YP_145021.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71578; BAD71578; BAD71578.
GeneIDi3169449.
KEGGittj:TTHA1755.
PATRICi23958473. VBITheThe93045_1726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71578.1.
RefSeqiWP_011228893.1. NC_006461.1.
YP_145021.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VEFX-ray1.35A/B1-395[»]
1WKGX-ray2.25A/B1-395[»]
1WKHX-ray2.25A/B1-395[»]
ProteinModelPortaliQ5SHH5.
SMRiQ5SHH5. Positions 9-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1755.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71578; BAD71578; BAD71578.
GeneIDi3169449.
KEGGittj:TTHA1755.
PATRICi23958473. VBITheThe93045_1726.

Phylogenomic databases

eggNOGiENOG4105C8Y. Bacteria.
COG4992. LUCA.
HOGENOMiHOG000020206.
KOiK05830.
OMAiFSEIRGM.
PhylomeDBiQ5SHH5.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00038.
UPA00068; UER00109.
BioCyciTTHE300852:GH8R-1797-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHH5.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3. 1 hit.
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...

Entry informationi

Entry nameiARGD_THET8
AccessioniPrimary (citable) accession number: Q5SHH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.