Skip Header

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

Q7VAS9 (ARGD_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:Pro_1375
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length419 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.

Sequence caution

The sequence AAQ00419.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112765

Regions

Region240 – 2434Pyridoxal phosphate binding By similarity

Sites

Binding site1491Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1521N2-acetyl-L-ornithine By similarity
Binding site2961N2-acetyl-L-ornithine By similarity
Binding site2971Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VAS9 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: DC0F95691ED5C975

FASTA41946,354
        10         20         30         40         50         60 
MVDAPHSKCG TFGFVGSSPT APTFLLDTYK RLPLKIVKGN GCWLWDETGK KYLDAVAGIA 

        70         80         90        100        110        120 
TCSLGHSDKK LSKVLSQQLR KIQHVSNLYR IPEQEDLAQW LVNQSCADSV FFCNSGAEAN 

       130        140        150        160        170        180 
EAAIKLARKY GQIKRGIKRP IILSAKSSFH GRTLAALSAT GQTKYQKGFE PLVEGFEFFS 

       190        200        210        220        230        240 
FNDSNSVQDL YENLEKDEPR VAAILIEPIQ GEGGLNLGDQ KFFYFLRDYC NKNNILLLFD 

       250        260        270        280        290        300 
EVQSGMGRTG KLWGYEHFNV EPDAFTLAKG LGGGHSIGAL LVKENASIFE PGDHASTFGG 

       310        320        330        340        350        360 
NPFACKAGLT VAKEIQNRNL LENTYCRGNQ LREGLQKLIN NYPHHLEEVR GIGLMLGLAI 

       370        380        390        400        410 
KKNSNLTSQK IVELAIKEGL LVIGAGEKVI RMLPPLIITK REIETLLTRL NACFRKLNN 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed: 12917486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAQ00419.1. Different initiation.
RefSeqNP_875766.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7VAS9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1462756.
GenomeReviewsGene locus Pro_1375 in contig AE017126_GR.
KEGGpma:Pro1375.
PATRIC23029515. VBIProMar8617_1442.

Phylogenomic databases

HOGENOMHBG725944.
OMAPLVMTKE.
ProtClustDBPRK02627.

Enzyme and pathway databases

BioCycPMAR167539:PRO_1375-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_PROMA
AccessionPrimary (citable) accession number: Q7VAS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 5, 2009
Last modified: January 25, 2012
This is version 64 of the entry and version 2 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