P59320 (ARGD_SHEON) 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:	SO_0617

Organism

Shewanella oneidensis

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

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 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 – 405	405	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112778
Regions
	Region	225 – 228	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	140	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	143	1	N2-acetyl-L-ornithine By similarity
	Binding site	282	1	N2-acetyl-L-ornithine By similarity
	Binding site	283	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59320 [UniParc]. Last modified February 12, 2003. Version 1. Checksum: 5EF6879ED99283E0	FASTA	405	43,214
	10 20 30 40 50 60 MSVDMKLNRA QFDAVMVPNY APAAVIPVRG EGSRVWDQEG NEFIDFAGGI AVNCLGHCHP 70 80 90 100 110 120 ALVNALKTQG EKLWHLSNVM TNEPALELAT KLVNSTFAER VYFANSGAEA NEAALKLARR 130 140 150 160 170 180 YALEKHGVEK DEIIAFDKAF HGRTFFTVSV GGQAAYSDGF GPKPQSITHL PFNDVAALEA 190 200 210 220 230 240 AVSDKTCAIM LEPLQGEGGI IDADPAFLKA VRELANKHNA LVIFDEVQTG VGRTGELYAY 250 260 270 280 290 300 MGTDIVPDIL TTAKALGGGF PIAAMLTTTE IAEHLKVGTH GSTYGGNPLA CAIGNAVLDV 310 320 330 340 350 360 VNTPEVLNGV KHREQLLRDG LNKINEKYHV FSEVRGKGLL LGAVLNEQYQ GRSRDFLVAS 370 380 390 400 VAEGLMSLMA GANVVRFAPS LVIPEADIAE GLARFERAVA SIAAA

References

[1]

"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014299 Genomic DNA. Translation: AAN53695.1.
RefSeq	NP_716250.1. NC_004347.1.
3D structure databases
ProteinModelPortal	P59320.
SMR	P59320. Positions 17-402.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1168483.
GenomeReviews	Gene locus SO_0617 in contig AE014299_GR.
KEGG	son:SO_0617.
NMPDR	fig|211586.1.peg.578.
PATRIC	23520922. VBISheOne101494_0595.
TIGR	SO_0617.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	YADGFGP.
ProtClustDB	PRK05093.
Enzyme and pathway databases
BioCyc	SONE211586:SO_0617-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_SHEON

Accession

Primary (citable) accession number: P59320

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program