Q9CC12 (ARGD_MYCLE) 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:	ML1409

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	404 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 – 404	404	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112755
Regions
	Region	113 – 114	2	Pyridoxal phosphate binding By similarity
	Region	224 – 227	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	139	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	142	1	N2-acetyl-L-ornithine By similarity
	Binding site	281	1	N2-acetyl-L-ornithine By similarity
	Binding site	282	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	253	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CC12 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A9465B243A4570B6	FASTA	404	42,007
	10 20 30 40 50 60 MTPTQTNTAT MQQRWETVMM NNYGTPPIVL ASGNGAVVTD VDSNTYLDLL GGIAVNVLGH 70 80 90 100 110 120 RHPAVIEAVT HQITTLGHTS NLYATEPSIT LAEELVALLG ADTQTRVFFC NSGTEANELA 130 140 150 160 170 180 FKLSRLTGRT KLVAAQAAFH GRTMGSLALT GQPAKQAAFE PLPGHVTHVP YGQVDALAAA 190 200 210 220 230 240 VDNDTAAVFL EPIMGESGVI VPPEGYLAAA RDITTRHGAL LVIDEVQTGI GRTGAFFAHQ 250 260 270 280 290 300 HDSITPDVVT LAKGLGGGLP IGAFLATGPA AELLTLGLHG STFGGNPVCT AAALAVLRVL 310 320 330 340 350 360 ATQGLVRRAE VLGDSMRIGI ESLSHPLIDQ VRGRGLLLGI VLTAPRAKDI EKAARDAGFL 370 380 390 400 VNATAPEVIR LAPPLIITES QIDSFITALP GILDASIAEL GKKA

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL583922 Genomic DNA. Translation: CAC30360.1.
PIR	C87085.
RefSeq	NP_302002.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q9CC12.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028386; EBMYCP00000027992; EBMYCG00000028381.
GeneID	910549.
GenomeReviews	Gene locus ML1409 in contig AL450380_GR.
KEGG	mle:ML1409.
NMPDR	fig|272631.1.peg.874.
PATRIC	18055362. VBIMycLep78757_2614.
Organism-specific databases
Leproma	ML1409.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015339.
HOGENOM	HBG725944.
OMA	FEYQAHE.
ProtClustDB	PRK03244.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1409-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_MYCLE

Accession

Primary (citable) accession number: Q9CC12

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program