Reviewed, UniProtKB/Swiss-Prot Q7N9E5 (ARGD_PHOLL)

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:	plu0394

Organism

Photorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP]

Taxonomic identifier

141679 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

Protein attributes

Sequence length	403 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-2,6-diaminopimelate from (S)-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 – 403	403	Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107		PRO_0000112764
Regions
	Region	225 – 228	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	140	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	143	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	282	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7N9E5-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 1C975E88FAA0B5E1	FASTA	403	43,664
	10 20 30 40 50 60 MKEHIAVDRN TYDQVMLPIY SPAQFIPVRG QGSRVWDQHG KEYIDFAGGI AVVALGHCHP 70 80 90 100 110 120 TLVDVLKQQG EKLWHISNIF TNEPALILAQ KLIDATFAER VFFANSGAEA NEAAFKLARH 130 140 150 160 170 180 YAIARHNPYK TKIIAFHQGF HGRTLFTVSV GGQPKYADGF GPKPADIIHV PFNDLDAVKA 190 200 210 220 230 240 VIDDHTCAVV LEPVQGEGGV TAAAPAFIHG VRELCDKHQV LLVFDEVQSG MGRTGKLFSY 250 260 270 280 290 300 MHYDVTPDII TTAKALGNGF PISAMLTTVN IASVMTPGAH GTTYGGNPLA CAVANVAFDI 310 320 330 340 350 360 INTPAVLAGV EKRHNLMVNF LNDINQKYSI FGEIRGKGLL IGAELKAPHQ GKAKDILQLA 370 380 390 400 AENGLMLLSA GGDVLRFTPS LIISEEEIAQ GMERLEQVIN QLV

References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens." Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. , Siguier P., Vincent R., Wingate V., Zouine M., Glaser P., Boemare N., Danchin A., Kunst F. Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TT01.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571860 Genomic DNA. Translation: CAE12689.1.
RefSeq	NP_927747.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2800344.
GenomeReviews	Gene locus plu0394 in contig BX470251_GR.
KEGG	plu:plu0394.
NMPDR	fig|243265.1.peg.371.
Organism-specific databases
PhotoList	plu0394.
CMR	Search...
Phylogenomic databases
HOGENOM	Q7N9E5.
OMA	EHNALLV.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU0394-MON.
BRENDA	2.6.1.11. 308689. 2.6.1.17. 308689.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. 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_PHOLL

Accession

Primary (citable) accession number: Q7N9E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	December 15, 2003
Last modified:	November 3, 2009
This is version 50 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)