Q9LCS5 (ARGD_STRCL) 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

Organism

Streptomyces clavuligerus

Taxonomic identifier

1901 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	400 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
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 – 400	400	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112799
Regions
	Region	217 – 220	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	132	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	135	1	N2-acetyl-L-ornithine By similarity
	Binding site	274	1	N2-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)
	Q9LCS5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2098C14DF9359C2C	FASTA	400	41,968
	10 20 30 40 50 60 MSNQEFAQRW QGVMIDSYGT PGLSFVRGEG STLWDADGTA YTDFVSGLAV NALGHAHPAV 70 80 90 100 110 120 VGAVSRQIAS LGHISNFYSA EPTITLAERL IELFGRPGRV FFCNSGAEAN ETAFKIGRLT 130 140 150 160 170 180 GRSRIVAAQS GFHGRTMGSL ALTGQPAKRE PFLPLPGDVT HVPYGDAEAL RAAVTEDTAM 190 200 210 220 230 240 VILEPIQGES GVVVPPKGYL RAAREITEAT GTLLVLDEVQ TGIGRTGHWF AAQAEGVEAD 250 260 270 280 290 300 VVTLAKGLGG GLPLGAAVAF GRAAELMTPG HHASTFGGNP VSCARTRVLD TIAADGLLDR 310 320 330 340 350 360 VKQLGSAPDE WSVRDAAAIR WSPMSGAGLM LGIVLNEPLA PQVQLAAQKA GFLVNVPAPD 370 380 390 400 VVRLIPPLVI EETEVDAFLQ ALPGLLDAVH ERDREGQTGE

References

[1]	"Characterization and expression of the arginine biosynthesis gene cluster of Streptomyces clavuligerus." Rodriguez-Garcia A., de la Fuente A., Perez-Redondo R., Martin J.F., Liras P. J. Mol. Microbiol. Biotechnol. 2:543-550(2000) [PubMed: 11075930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49111 Genomic DNA. Translation: CAB82482.1.
3D structure databases
ProteinModelPortal	Q9LCS5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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_STRCL

Accession

Primary (citable) accession number: Q9LCS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	September 21, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program