Q59282 (ARGD_CORGL) 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:	Cgl1397, cg1583

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	391 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 – 391	391	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112741
Regions
	Region	224 – 227	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	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
Experimental info
	Sequence conflict	267 – 268	2	TG → L in CAA60099. Ref.1
	Sequence conflict	267 – 268	2	TG → L in AAC24815. Ref.2
	Sequence conflict	312 – 313	2	GE → Q in CAA60099. Ref.1
	Sequence conflict	312 – 313	2	GE → Q in AAC24815. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q59282 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 10EF51CAC4FE1A1B	FASTA	391	41,206
	10 20 30 40 50 60 MSTLETWPQV IINTYGTPPV ELVSGKGATV TDDQGNVYID LLAGIAVNAL GHAHPAIIEA 70 80 90 100 110 120 VTNQIGQLGH VSNLFASRPV VEVAEELIKR FSLDDATLAA QTRVFFCNSG AEANEAAFKI 130 140 150 160 170 180 ARLTGRSRIL AAVHGFHGRT MGSLALTGQP DKREAFLPMP SGVEFYPYGD TDYLRKMVET 190 200 210 220 230 240 NPTDVAAIFL EPIQGETGVV PAPEGFLKAV RELCDEYGIL MITDEVQTGV GRTGDFFAHQ 250 260 270 280 290 300 HDGVVPDVVT MAKGLGGGLP IGACLATGRA AELMTPGKHG TTFGGNPVAC AAAKAVLSVV 310 320 330 340 350 360 DDAFCAEVAR KGELFKELLA KVDGVVDVRG RGLMLGVVLE RDVAKQAVLD GFKHGVILNA 370 380 390 PADNIIRLTP PLVITDEEIA DAVKAIAETI A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway." Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N., Hallet J.-N., Glansdorff N. Microbiology 142:99-108(1996) [PubMed: 8581175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"Molecular cloning of the arginine biosynthetic genes from Corynebacterium glutamicum." Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[3]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X86157 Genomic DNA. Translation: CAA60099.1. AF049897 Genomic DNA. Translation: AAC24815.1. BA000036 Genomic DNA. Translation: BAB98790.1. BX927152 Genomic DNA. Translation: CAF21408.1.
RefSeq	NP_600616.1. NC_003450.3. YP_225684.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q59282.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019373. 3344455.
GenomeReviews	Gene locus Cgl1397 in contig BA000036_GR. Gene locus cg1583 in contig BX927147_GR.
KEGG	cgb:cg1583. cgl:NCgl1343.
PATRIC	21494833. VBICorGlu203724_1366.
Phylogenomic databases
HOGENOM	HBG725944.
OMA	THIWHTS.
PhylomeDB	Q59282.
ProtClustDB	PRK03244.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1583-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_CORGL

Accession

Primary (citable) accession number: Q59282

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2002
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program