Reviewed, UniProtKB/Swiss-Prot P57600 (ARGD_BUCAI)

Names and origin

Protein names

Recommended name:
    Acetylornithine/succinyldiaminopimelate aminotransferase
      Short name=ACOAT
      Short name=Succinyldiaminopimelate transferase
      Short name=DapATase
    EC=2.6.1.11
    EC=2.6.1.17

Gene names

Name:	argD
Synonyms:	dapC
Ordered Locus Names:	BU534

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways By similarity.
Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107 N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107 Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-diaminopimelate from tetrahydrodipicolinate (succinylase route): step 2/3. HAMAP MF_01107
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine 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: HAMAP lysine 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: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro succinyldiaminopimelate transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 408	408	Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107		PRO_0000112734
Regions
	Region	226 – 229	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	141	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	144	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	284	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57600-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 6278FD811211F419	FASTA	408	45,295
	10 20 30 40 50 60 MISKKTLITR DNFDKLILPI YNPIPFIPIK GKGSRIWDQK GKEYIDFSGG IAVTSLGHCH 70 80 90 100 110 120 PILNKTLKNQ SKMLWHLSNI FTNEPALRLA KKLLSSSFAS RIFFANSGAE ANEAAFKLAR 130 140 150 160 170 180 YYSSKIYNFK KNKIISFYNS FHGRTFFTVS VGGQSKYSNN FGPKPAGIVH ASFNDINSVK 190 200 210 220 230 240 NLIDHDTCAV VVELIQGEGG VIPANLTFVQ ALKELCKQYN VLLIFDEIQT GIGRTGKLFY 250 260 270 280 290 300 YEYYAITPDI LTIAKSLGGG FPISAMLTTN EVASVIAPGI HGTTYGGNPL ACAVAESVID 310 320 330 340 350 360 IINTKKVLSG VEKKSKKIIS ELNIINKRFK LFTEIRGRGL LIGIVLKPNV SRNIHKILNF 370 380 390 400 SLSEGVIFLT AGNNVIRLAP SLIIKELDII EGMKRFYRAL EKYLSRKE

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB13227.1.
RefSeq	NP_240341.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1109877.
GenomeReviews	Gene locus BU534 in contig BA000003_GR.
KEGG	buc:BU534.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57600.
OMA	P57600. EHNALLV.
Enzyme and pathway databases
BioCyc	BSP107806:BU534-MON.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR005814. Aminotrans_3. IPR004636. ArgD_aminotrans. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR017652. SuccinylOrn_transaminase. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR03246. arg_catab_astC. 1 hit. TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_BUCAI

Accession

Primary (citable) accession number: P57600

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)