P59319 (ARGD_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	PP_4481

Organism

Pseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]

Taxonomic identifier

160488 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	406 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 – 406	406	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112769
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)
	P59319 [UniParc]. Last modified February 12, 2003. Version 1. Checksum: 5597D2F10C3E221E	FASTA	406	43,490
	10 20 30 40 50 60 MSVEQAPVQR ADFDQVMVPN YSPAAFIPVR GEGSRVWDQS GRELIDFAGG IAVNALGHCH 70 80 90 100 110 120 PALVKALTEQ ANTLWHVSNV FTNEPALRLA HKLVDATFAD RAFFCNSGAE SNEAAFKLAR 130 140 150 160 170 180 RVAHDRFGPQ KHEIIATVNS FHGRTLFTVS VGGQPKYSDG FGPKITGISH VPYNDLEALK 190 200 210 220 230 240 AQISDKTCAV VIEPIQGESG VVPADKAYLE GARKLCDEHN ALLIFDEVQT GVGRTGSLYA 250 260 270 280 290 300 YQHYGVIPDI LTSAKSLGGG FPIGAMLTTT ELAKHLAVGT HGTTYGGNPL GCAVACAVLD 310 320 330 340 350 360 VVNTPETLAG IKAKHERFKT RLEQIGQQYN LFSQVRGVGL LLGCVLTEAW KGKAKDVLNA 370 380 390 400 AEKEGVMVLQ AGPDVVRFAP SLVVEDADID EGLDRFERAV ATLTKG

References

[1]

"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440." Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O. , Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M. Environ. Microbiol. 4:799-808(2002) [PubMed: 12534463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KT2440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015451 Genomic DNA. Translation: AAN70056.1.
RefSeq	NP_746592.1. NC_002947.3.
3D structure databases
ProteinModelPortal	P59319.
SMR	P59319. Positions 18-403.
ModBase	Search...
Protein-protein interaction databases
STRING	P59319.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1041851.
GenomeReviews	Gene locus PP_4481 in contig AE015451_GR.
KEGG	ppu:PP_4481.
NMPDR	fig|160488.1.peg.4422.
PATRIC	19947660. VBIPsePut30601_4767.
TIGR	PP_4481.
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HBG725944.
OMA	ERTRVIT.
PhylomeDB	P59319.
ProtClustDB	PRK05093.
Enzyme and pathway databases
BioCyc	PPUT160488:PP_4481-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

ARGD_PSEPK

Accession

Primary (citable) accession number: P59319

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program