Q9L1A4 (ARGD_STRCO) 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:	SCO1577
ORF Names:	SCL24.13c

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	402 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 – 402	402	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112800
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	275	1	N2-acetyl-L-ornithine By similarity
	Binding site	276	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	247	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9L1A4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1A15CC13A233129F	FASTA	402	41,560
	10 20 30 40 50 60 MSNEELTERW QGTLMNNYGT PRLPLVRGEG ARLWDADGKE YLDFVGGIAV NALGHAHPAV 70 80 90 100 110 120 VDAVSRQIAS LGHVSNLFIA EPPVALAERL LQHFGRDGKV YFCNSGAEAN EGAFKIGRLT 130 140 150 160 170 180 GRPHMVATRG GFHGRTMGAL ALTGQPGKQE PFLPLPGDVT HVPYGDPQAL AAAVTEETAL 190 200 210 220 230 240 VIIEPIQGEN GVVVPPPGYL KAARAITAAT GALLVLDEVQ TGVGRTGHWF EYQAHEGVLP 250 260 270 280 290 300 DVVTLAKGLG GGLPLGATVA FGRAADLLQP GHHGTTFGGN PVACAAGLAV LDTIADEGLL 310 320 330 340 350 360 DNVKRQSETL RGGVEALGHP LVAHVRGAGL LLGIVLTEPL AAQVQQAAQD AGILVNAPAP 370 380 390 400 DVVRLMPALN LGDDVVEAFL GALPGILDQA AETAHGDGRS GE

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939109 Genomic DNA. Translation: CAB76097.1.
RefSeq	NP_625854.1. NC_003888.3.
3D structure databases
ProteinModelPortal	Q9L1A4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1097008.
GenomeReviews	Gene locus SCO1577 in contig AL645882_GR.
KEGG	sco:SCO1577.
NMPDR	fig|100226.1.peg.1544.
PATRIC	23732750. VBIStrCoe124346_1589.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	FEYQAHE.
PhylomeDB	Q9L1A4.
ProtClustDB	PRK03244.
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_STRCO

Accession

Primary (citable) accession number: Q9L1A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
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