Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q92BC0 (ARGD_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylornithine aminotransferase

Short name=ACOAT
EC=2.6.1.11
Gene names
Name:argD
Ordered Locus Names:lin1630
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107

Subunit structure

Homodimer By similarity. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107

Sequence similarities

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

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112752

Regions

Region94 – 952Pyridoxal phosphate binding By similarity
Region206 – 2094Pyridoxal phosphate binding By similarity

Sites

Binding site1211Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1241N2-acetyl-L-ornithine By similarity
Binding site2631N2-acetyl-L-ornithine By similarity
Binding site2641Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92BC0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A37DC1EFCC411F0B

FASTA38441,336
        10         20         30         40         50         60 
MKHVFPTYNR FPVDIVKGNG TVVKDATGKT YLDFTSGIAV CNLGHCPENV TEAIQSQLAN 

        70         80         90        100        110        120 
IWHTSNLYEC ALQDSVAELI TDGTDKLVFF CNSGTEANEA ALKLARKYTG KEKIITFEKS 

       130        140        150        160        170        180 
FHGRTFGSMS ATGQAKIHQG FGRLVPGFTY VPYNDIESFK TELDENTAAV MLEVIQGEGG 

       190        200        210        220        230        240 
VIPGNAAWLM EVQMLCKKAG ALLIIDEVQT GLGRTGTLFG FQQTFLDPDI FTLAKGLGNG 

       250        260        270        280        290        300 
LPIGAMVGKE HLSSAFGPGS HGSTFGGNKL ALAAAKEILL TMKQTGFLEE VNAKAAYFRN 

       310        320        330        340        350        360 
LLEEHFEQLE NVVAIRGEGF LIGIELGSSA APVVTELRDK GLLILTAGPN ILRILPPLTV 

       370        380 
SYAEIDQAIS ILKSVLEKQL IGSE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596169 Genomic DNA. Translation: CAC96861.1.
PIRAE1636.
RefSeqNP_470966.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ92BC0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1130253.
GenomeReviewsGene locus lin1630 in contig AL592022_GR.
KEGGlin:lin1630.
NMPDRfig|272626.1.peg.1619.
PATRIC20299997. VBILisInn102668_1665.

Organism-specific databases

GenoListLIN1630.
CMRSearch...

Phylogenomic databases

HOGENOMHBG725944.
OMAGAMIGKA.
ProtClustDBPRK02936.

Enzyme and pathway databases

BioCycLINN272626:LIN1630-MONOMER.

Family and domain databases

HAMAPMF_01107. ArgD_aminotrans_3.
[Tree]
InterProIPR004636. AcOrn/SuccinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00818.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00707. ArgD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_LISIN
AccessionPrimary (citable) accession number: Q92BC0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families