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Reviewed, UniProtKB/Swiss-Prot P54752 (ARGD_ANASP)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
Gene names
Name: argD
Ordered Locus Names: alr1080
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm Probable.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112714

Regions

Region248 – 2514Pyridoxal phosphate binding By similarity

Sites

Binding site1571Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1601N(2)-acetyl-L-ornithine By similarity
Binding site3041N(2)-acetyl-L-ornithine By similarity
Binding site3051Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2771N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P54752-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6AF594BB4B3B134E

FASTA42746,140
        10         20         30         40         50         60 
MSLQTLIEQA TNPPESGSAA SSPFSTDSFD ASVMSTYGRF PLALERGAGC RVWDTQGKEY 

        70         80         90        100        110        120 
LDFVAGIATC TLGHAHPAMV EAVTRQIQKL HHVSNLYYIP EQGELAQWII QHSCADRVFF 

       130        140        150        160        170        180 
CNSGAEANEA AIKLARKYAH TVLDIEKPII LTANASFHGR TLATITATGQ AKYQKYFDPL 

       190        200        210        220        230        240 
VPGFHYVNYN DISAVEAAIS ELDEGDYRVA AILIEPLQGE GGVRPGDVEY FQKLRQICDD 

       250        260        270        280        290        300 
TGILLMFDEV QVGMGRSGKL WGYEYLGVEP DIFTSAKGLG GGIPIGAMMS KKFCDVFQPG 

       310        320        330        340        350        360 
EHASTFGGNP FACGVALAVC QTLERENILQ NVQDRGEQLR SGLRAIAAKY PHHLTEVRGW 

       370        380        390        400        410        420 
GLINGLELAA DIPLTAADVV KAAINEGLLL VPAGPKVVRF VPPLIVTEAE INTALKLLEK 


ALATVTA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of expression of the argC and argD genes in the cyanobacterium Anabaena sp. strain PCC 7120."
Floriano B., Herrero A., Flores E.
J. Bacteriol. 176:6397-6401(1994) [PubMed: 7929012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

X78854 Genomic DNA. Translation: CAA55410.1.
BA000019 Genomic DNA. Translation: BAB73037.1.
PIRAE1941.
RefSeqNP_485123.1.

3D structure databases

HSSPHSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBaseSearch...

Genome annotation databases

GeneID1104674.
GenomeReviewsGene locus alr1080 in contig BA000019_GR.
KEGGana:alr1080.
NMPDRfig|103690.1.peg.1390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP54752.
OMAP54752. EHNALLV.

Enzyme and pathway databases

BioCycNSP103690:ALR1080-MON.

Family and domain databases

HAMAPMF_01107.
[Tree]
InterProIPR005814. Aminotrans_3.
IPR004636. ArgD_aminotrans.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00707. argD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_ANASP
AccessionPrimary (citable) accession number: P54752
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents