Q828A3 (ARGD_STRAW) 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:	SAV_6766

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	403 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 – 403	403	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112798
Regions
	Region	221 – 224	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	136	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	139	1	N2-acetyl-L-ornithine By similarity
	Binding site	279	1	N2-acetyl-L-ornithine By similarity
	Binding site	280	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	251	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q828A3 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 14734A54E1BD048D	FASTA	403	41,670
	10 20 30 40 50 60 MTGTATNAEL TERWQGALMN NYGTPRLPLV RGAGTRLWDA DGKEYLDFVG GIAVNALGHA 70 80 90 100 110 120 HPAIVEAVST QIASLGHVSN LFVAEPPVAL AERLLQLFGR DGRVYFCNSG AEANEAAFKI 130 140 150 160 170 180 GRLTGRSHMV ATQGGFHGRT MGALALTGQP GKQEPFLPLP GDVTHVPYGD AQALAAAVTE 190 200 210 220 230 240 ETALVVIEPI QGENGVVVPP AGYLKAARAI TAATGSLLVL DEVQTGIGRT GHWFEYQAHE 250 260 270 280 290 300 GVLPDVVTLA KGLGGGLPLG ATVAFGRAAE LLQPGHHGTT FGGNPIACAA GLAVLETIQA 310 320 330 340 350 360 EGLLENVKSA SEKLRDGIES LGHPLIAHVR GSGLLLGIVL TEPLAPQAQQ AAQDAGFLVN 370 380 390 400 APAPDVVRLM PPLNLGDDEV DAFLRALPGV LDAVTNGDGR AKE

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC74477.1.
RefSeq	NP_827942.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q828A3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1211557.
GenomeReviews	Gene locus SAV_6766 in contig BA000030_GR.
KEGG	sma:SAV_6766.
NMPDR	fig|227882.1.peg.6768.
PATRIC	23727646. VBIStrAve112782_7172.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	FEYQAHE.
ProtClustDB	PRK03244.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV6766-MONOMER.
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. 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	K00818.
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	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_STRAW

Accession

Primary (citable) accession number: Q828A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program