Reviewed, UniProtKB/Swiss-Prot Q82UP3 (ARGD_NITEU)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	NE1439

Organism

Nitrosomonas europaea [Complete proteome] [HAMAP]

Taxonomic identifier

915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas

Protein attributes

Sequence length	393 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
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
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: HAMAP 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 – 393	393	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112761
Regions
	Region	214 – 217	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	127	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	130	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	271	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	272	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	243	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82UP3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 9BF3CC7977016064	FASTA	393	43,074
	10 20 30 40 50 60 MSHVMNTYAR LPVTFVKGEG VWLWDDQGNR YLDALSGIAV CGVGHCHPVL VKALCEQVST 70 80 90 100 110 120 LIHTSNVYHI QHQERLADRL TSLSGLEKAF FCNSGAEANE AAIKLARLYG HNQGINLPTI 130 140 150 160 170 180 IVMERSFHGR TMATLTATGN RKTQAGFEPL LTGFVRVPYD DLEAVNKVAA NNREIVAILL 190 200 210 220 230 240 ETYQGEGGVN FPQANYLQGL RRICDQNGWL LMLDEVQCGL GRTGKWFAFQ HSEVMPDAMT 250 260 270 280 290 300 LAKGLGSGVP IGACLAGGKA AEVFKPGNHA STFGGNPLAC RAALTTLDII EQEGLMDNAV 310 320 330 340 350 360 TIGNFMWEEF GRRLQAWQDV LKIRGQGMMI GIELPVPCSE LVPEALKRRV LVNVTSEKVV 370 380 390 RLLPALNMQK AEAEQVVTEV SALITWFLES RVK

References

[1]

"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea." Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J. J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19718 / IFO 14298.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL954747 Genomic DNA. Translation: CAD85350.1.
RefSeq	NP_841480.1.
3D structure databases
SMR	Q82UP3. Positions 2-381.
ModBase	Search...
Genome annotation databases
GeneID	1082389.
GenomeReviews	Gene locus NE1439 in contig AL954747_GR.
KEGG	neu:NE1439.
NMPDR	fig|228410.1.peg.1379.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	LMIAIEL.
Enzyme and pathway databases
BioCyc	NEUR228410:NE1439-MONOMER.
BRENDA	2.6.1.11. 444.
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. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_NITEU

Accession

Primary (citable) accession number: Q82UP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)