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O08321 (ARGD_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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:lp_0531
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length389 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112749

Regions

Region96 – 972Pyridoxal phosphate binding By similarity
Region207 – 2104Pyridoxal phosphate binding By similarity

Sites

Binding site1231Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1261N2-acetyl-L-ornithine By similarity
Binding site2641N2-acetyl-L-ornithine By similarity
Binding site2651Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict2781C → R in CAA68242. Ref.1
Sequence conflict2811P → T in CAA68242. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08321 [UniParc].

Last modified November 16, 2011. Version 4.
Checksum: 428AEA97EA37C9C4

FASTA38941,459
        10         20         30         40         50         60 
MTMQHVFPTY QRFPFAITDG QGVHLTDNHG KTYLDFTAGI GVCNFGYHQP QIQAAVTQQL 

        70         80         90        100        110        120 
THIWHTSNLY ENELQDAVAG LLANGEERLV YFANSGTEAN EAALKLARKY TGKTGILAFQ 

       130        140        150        160        170        180 
HSFHGRTYGA MSMTGNPHIQ AGYAPLVPGI TFATYNDDAA LDKITPELAA VILEVVQGEG 

       190        200        210        220        230        240 
GVFAGQTAWL QAVNAKCQAT GVLLIIDEVQ TGIGRTGYRM AYEGYGLDPD IYTVAKGLAN 

       250        260        270        280        290        300 
GLPVGAMVGR RQLATAFGPG SHGSTFAGNA VAMAAAKCVL PQLTPALLTT VRAHAKLVWQ 

       310        320        330        340        350        360 
SLATQVEPIP VVKQITGKGL MIGIHLDEQI PVNQVITRLQ VEGLLTLSAG DNTLRLLPPI 

       370        380 
VMQPADLLAG IALIAKVLTT LTTEVTTNE 

« Hide

References

« Hide 'large scale' references
[1]"Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA gene and the argCJBDF cluster are divergently transcribed."
Bringel F., Frey L., Boivin S., Hubert J.-C.
J. Bacteriol. 179:2697-2706(1997) [PubMed: 9098069] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376.
[2]"Complete genome sequence of Lactobacillus plantarum WCFS1."
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99978 Genomic DNA. Translation: CAA68242.1.
AL935263 Genomic DNA. Translation: CCC78021.1.
RefSeqNP_784309.1. NC_004567.1.

3D structure databases

ProteinModelPortalO08321.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1061852.
GenomeReviewsGene locus lp_0531 in contig AL935263_GR.
KEGGlpl:lp_0531.
NMPDRfig|220668.1.peg.443.
PATRIC22247505. VBILacPla27411_0439.

Phylogenomic databases

HOGENOMHBG725944.
ProtClustDBPRK02936.

Enzyme and pathway databases

BioCycLPLA220668:LP_0531-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_LACPL
AccessionPrimary (citable) accession number: O08321
Secondary accession number(s): F9UL06
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 16, 2011
Last modified: January 25, 2012
This is version 90 of the entry and version 4 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