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Reviewed, UniProtKB/Swiss-Prot Q9PIR7 (ARGD_CAMJE)

Last modified November 3, 2009. Version 68. 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

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Names and origin

Protein namesRecommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
Gene names
Name: argD
Ordered Locus Names: Cj0227
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112736

Regions

Region100 – 1012Pyridoxal phosphate binding By similarity
Region217 – 2204Pyridoxal phosphate binding By similarity

Sites

Binding site1321Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1351N(2)-acetyl-L-ornithine By similarity
Binding site2751N(2)-acetyl-L-ornithine By similarity
Binding site2761Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2461N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict10 – 123IPT → VPA in AAF21805. Ref.1
Sequence conflict1201V → I in AAF21805. Ref.1
Sequence conflict3411S → N in AAF21805. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9PIR7-1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 62AE74E1696FFC55

FASTA39343,519
        10         20         30         40         50         60 
MDYKEQSHII PTYKRFDIVL EKGQGVYLFD DKAKKYLDFS SGIGVCALGY NHAKFNAKIK 

        70         80         90        100        110        120 
AQVDKLLHTS NLYYNENIAA AAKNLAKASA LERVFFTNSG TESIEGAMKT ARKYAFNKGV 

       130        140        150        160        170        180 
KGGQFIAFKH SFHGRTLGAL SLTANEKYQK PFKPLISGVK FAKYNDISSV EKLVNEKTCA 

       190        200        210        220        230        240 
IILESVQGEG GINPANKDFY KALRKLCDEK DILLIADEIQ CGMGRSGKFF AYEHAQILPD 

       250        260        270        280        290        300 
IMTSAKALGC GLSVGAFVIN QKVASNSLEA GDHGSTYGGN PLVCAGVNAV FEIFKEEKIL 

       310        320        330        340        350        360 
ENVNKLTPYL EQSLDELINE FDFCKKRKGL GFMQGLSLDK SVKVAKVIQK CQENALLLIS 

       370        380        390 
CGENDLRFLP PLILQKEHID EMSEKLRKAL KSF

« Hide

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References

« Hide 'large scale' references
[1]"Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of the argCOBD cluster."
Hani E.K., Ng D., Chan V.-L.
Can. J. Microbiol. 45:959-969(1999) [PubMed: 10588044] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43431 / TGH 9011 / Serotype O:3.
[2]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

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Cross-references

Sequence databases

AL111168 Genomic DNA. Translation: CAL34382.1. Different initiation.
AF093219 Genomic DNA. Translation: AAF21805.1. Different initiation.
PIRC81440.
RefSeqYP_002343670.1.

3D structure databases

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

Protein-protein interaction databases

IntActQ9PIR7. 13 interactions.

Genome annotation databases

GeneID904555.
GenomeReviewsGene locus Cj0227 in contig AL111168_GR.
KEGGcje:Cj0227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEHIDEMS.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0227-MON.
BRENDA2.6.1.11. 255835.

Family and domain databases

HAMAPMF_01107.
[Tree]
InterProIPR004636. AcOrn/succinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
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...

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Entry information

Entry nameARGD_CAMJE
AccessionPrimary (citable) accession number: Q9PIR7
Secondary accession number(s): Q0PBS7, Q9RGZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 5, 2009
Last modified: November 3, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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