NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

Comments

FUNCTION: Involved in both the arginine and lysine biosynthetic pathways (By similarity).
CATALYTIC ACTIVITY: N²-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CATALYTIC ACTIVITY: N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate.
COFACTOR: Pyridoxal phosphate (By similarity).
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4 .
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-diaminopimelate from tetrahydrodipicolinate (succinylase route): step 2/3 .
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000003; BAB13227.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_240341.1; -.

3D structure databases

HSSP

P12995; 1QJ3. [HSSP ENTRY / PDB]

ModBase

P57600.

Enzyme and pathway databases

BioCyc

BSP107806:BU534-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003992;	Molecular function: acetylornithine transaminase activity (inferred from electronic annotation from HAMAP).
GO:0009016;	Molecular function: succinyldiaminopimelate transaminase activity (inferred from electronic annotation from EC).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0009085;	Biological process: lysine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01107; -; 1.
PBIL [Tree]

InterPro

IPR005814; Aminotrans_3.
IPR004636; ArgD_aminotrans.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR017652; SuccinylOrn_transaminase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.

PANTHER

PTHR11986; Aminotrans_3; 1.
PTHR11986:SF19; ArgD_aminotrans; 1.

Pfam

PF00202; Aminotran_3; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00707; argD; 1.

PROSITE

PS00600; AA_TRANSFER_CLASS_3; 1.

Genome annotation databases

GeneID

1109877; -.

GenomeReviews

BA000003_GR; BU534.

KEGG

buc:BU534; -.

Phylogenomic databases

HOGENOM

P57600; -.

Genome annotation databases

CMR

P57600; BU534.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; Complete proteome; Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 408`	`408`	`Acetylornithine/succinyldiaminopimelate aminotransferase.`	`PRO_0000112734`
`BINDING`	`255 255`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 408 AA [This is the length of the unprocessed precursor]

Molecular weight: 45295 Da [This is the MW of the unprocessed precursor]

CRC64: 6278FD811211F419 [This is a checksum on the sequence]

        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

P57600 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools