Q885K0 (ARGD1_PSESM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylornithine aminotransferase 1
Short name=ACOAT 1
EC=2.6.1.11

Gene names

Name:	argD1
Ordered Locus Names:	PSPTO_1832

Organism

Pseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]

Taxonomic identifier

223283 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	405 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: 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 – 405	405	Acetylornithine aminotransferase 1 HAMAP MF_01107		PRO_0000112770
Regions
	Region	226 – 229	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	141	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	144	1	N2-acetyl-L-ornithine By similarity
	Binding site	283	1	N2-acetyl-L-ornithine By similarity
	Binding site	284	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q885K0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D2FF6E02563B829E	FASTA	405	43,432
	10 20 30 40 50 60 MSVEHAAVQR ADFDQVMVPN YAPAGFIPVR GAGSRVWDQA GRELVDFSGG IAVNVLGHCH 70 80 90 100 110 120 PALVGALTEQ ANNLWHVSNV FTNEPTLRLA KKLVDSTFAE RVFFCNSGAE ANEAAFKLAR 130 140 150 160 170 180 RVAHDLYGPE KYEIIAAVNS FHGRTLFTVS VGGQPKYSDG FGPKITGISH VPYNDLEALK 190 200 210 220 230 240 AAVTDKTCAV VLEPIQGEGG VLPGELDYLQ GARKLCDEHN ALLVFDEVQS GMGRSGHLFA 250 260 270 280 290 300 YMHYGVTPDI LSSAKSIGGG FPLAAMLTTE KLAKHFAVGV HGTTYGGNPL ACAVGEAVID 310 320 330 340 350 360 VINTPEVLAG VQRKHQQFKT RLESIGQQYG VFTEVRGLGL LIGCVLSDAW KGKAKDIFNA 370 380 390 400 AEAQDLMILQ AGPDVIRFAP SLVIEDADIE EGLNRFERAI AKLTS

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
EMBL GenBank DDBJ	AE016853 Genomic DNA. Translation: AAO55351.1.
RefSeq	NP_791656.1. NC_004578.1.
3D structure databases
ProteinModelPortal	Q885K0.
SMR	Q885K0. Positions 18-403.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1183473.
GenomeReviews	Gene locus PSPTO_1832 in contig AE016853_GR.
KEGG	pst:PSPTO_1832.
NMPDR	fig|223283.1.peg.1794.
PATRIC	19994930. VBIPseSyr93040_1862.
TIGR	PSPTO_1832.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	YADGFGP.
ProtClustDB	PRK05093.
Enzyme and pathway databases
BioCyc	PSYR223283:PSPTO_1832-MONOMER.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR017652. Ac/SuccinylOrn_transaminase. 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	TIGR03246. Arg_catab_astC. 1 hit. TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD1_PSESM

Accession

Primary (citable) accession number: Q885K0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program