Reviewed, UniProtKB/Swiss-Prot Q882K8 (ARGD2_PSESM)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase 2
      Short name=ACOAT 2
    EC=2.6.1.11

Gene names

Name:	argD2
Ordered Locus Names:	PSPTO_2618

Organism

Pseudomonas syringae pv. tomato [Complete proteome] [HAMAP]

Taxonomic identifier

323 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.

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 – 400	400	Acetylornithine aminotransferase 2 HAMAP MF_01107		PRO_0000112771
Regions
	Region	217 – 220	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	129	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	132	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	274	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	275	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	246	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q882K8-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4BC3FCA212FD1832	FASTA	400	43,225
	10 20 30 40 50 60 MTTACLMSTY QPLALSFTRG LGTRLWDQSG REYLDAVAGV AVTNVGHSHP MLVDAIRDQA 70 80 90 100 110 120 GLLLHTSNLY SIDWQQRLAQ KLTRLAGMDR VFFNNSGAEA NETALKLARL HGWHKYIEQP 130 140 150 160 170 180 LVVVMENAFH GRTLGTLAAS DGPAVRLSYS DLPGDYIKVP FGDLLAFDKV CVTHGHRIAA 190 200 210 220 230 240 VLVEPIQGEG GAQVAPAGYL KALRERCTRR DWLLMLDEIQ TGMGRTGKWF AFQHEGIVPD 250 260 270 280 290 300 VMTLAKGLGN GVPIGACLAR GKAAELFTPG SHGSTFGGNP LACRVGCTVI DIIEQQALVE 310 320 330 340 350 360 NAGVRGQHLL GRLQEVLGGH PQVMQVRGRG LMIGIELREA IPELTRIAAE QHGLLINVTR 370 380 390 400 GKVIRLLPPL VLEAAEVEQI VQGLAASLDS ASYRALERSA

References

[1]

"The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000." Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.M., Zafar N. , Zhou L., Liu J., Yuan Q., Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A. Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003) [PubMed: 12928499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DC3000.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016853 Genomic DNA. Translation: AAO56122.1.
RefSeq	NP_792427.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1184270.
GenomeReviews	Gene locus PSPTO_2618 in contig AE016853_GR.
KEGG	pst:PSPTO_2618.
NMPDR	fig|223283.1.peg.2565.
TIGR	PSPTO_2618.
Phylogenomic databases
HOGENOM	Q882K8.
OMA	YFAYQHT.
Enzyme and pathway databases
BioCyc	PSYR223283:PSPTO_2618-MON.
BRENDA	2.6.1.11. 289554.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. 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

ARGD2_PSESM

Accession

Primary (citable) accession number: Q882K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
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)