Acetylornithine aminotransferase - Agrobacterium tumefaciens (strain C58 / ATCC 33970)

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Q8UI71 (ARGD_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetylornithine aminotransferase
Short name=ACOAT
EC=2.6.1.11

Gene names

Name:	argD
Ordered Locus Names:	Atu0428
ORF Names:	AGR_C_752

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 399

399

Acetylornithine aminotransferase HAMAP MF_01107

PRO_0000112713

Regions

Region

217 – 220

Pyridoxal phosphate binding By similarity

Sites

Binding site

132

Pyridoxal phosphate; via carbonyl oxygen By similarity

Binding site

135

N2-acetyl-L-ornithine By similarity

Binding site

274

N2-acetyl-L-ornithine By similarity

Binding site

275

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

246

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8UI71 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: C715896DF031F4C4
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FASTA

399

42,478

        10         20         30         40         50         60 
MAEAAAPLFD TFARAPLRFE RGEGVWLFTE SGERYLDFAA GVAVNSLGHA HPHLVEAIKT 

        70         80         90        100        110        120 
QAEKVWHVSN LYEVPGQEKL AKRLTEATFA DKVFFTNSGA EALECAIKTA RRYHYSKGHP 

       130        140        150        160        170        180 
EKFRIITFEG AFHGRTLATI AAGGQQKYLE GFGPKVEGFD QVPFGDVDAL KAAITAETAA 

       190        200        210        220        230        240 
LLIEPIQGEG GIRAPAKEFL QLLRSLCDEH DLLLIFDEVQ TGVGRTGKFF AYEQTGVAPD 

       250        260        270        280        290        300 
IMAVAKGIGG GFPLGACLAT ADAASGMTAG VHGTTYGGNP LAMAVGNAVL DVVLADGFLE 

       310        320        330        340        350        360 
KVRDVALVFR QGLASLKDRY PDVIEEIRGE GLLLGIKARV PSGELLQAMR AEHLLGVPAG 

       370        380        390 
DNVIRLLPPL VTTAEEAREG LARVEAAAAS LTAKQAKIA

« Hide

References

[1]	"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.
[2]	"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK86241.1.
PIR	AB2629. H97410.
RefSeq	NP_353456.1. NC_003062.2.
3D structure databases
ProteinModelPortal	Q8UI71.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UI71.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1132466.
GenomeReviews	Gene locus Atu0428 in contig AE007869_GR.
KEGG	atu:Atu0428.
PATRIC	20810541. VBIAgrTum91616_0418.
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HBG725944.
OMA	GRKLWHI.
PhylomeDB	Q8UI71.
ProtClustDB	PRK01278.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU0428-MONOMER.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. 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]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K00821.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_AGRT5

Accession

Primary (citable) accession number: Q8UI71

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents