NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7929012 [NCBI, ExPASy, EBI, Israel, Japan]
Floriano B., Herrero A., Flores E.;
"Analysis of expression of the argC and argD genes in the cyanobacterium Anabaena sp. strain PCC 7120.";
J. Bacteriol. 176:6397-6401(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.;
"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.";
DNA Res. 8:205-213(2001).

Comments

CATALYTIC ACTIVITY: N²-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + 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 .
SUBCELLULAR LOCATION: Cytoplasm (Probable).
MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
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

X78854; CAA55410.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000019; BAB73037.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AE1941; AE1941.

RefSeq

NP_485123.1; -.

3D structure databases

HSSP

P12995; 1QJ3. [HSSP ENTRY / PDB]

ModBase

P54752.

Enzyme and pathway databases

BioCyc

NSP103690:ALR1080-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:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0006526;	Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
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.
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

1104674; -.

GenomeReviews

BA000019_GR; alr1080.

KEGG

ana:alr1080; -.

NMPDR

fig|103690.1.peg.1390; -.

Phylogenomic databases

HOGENOM

P54752; -.

Genome annotation databases

CMR

P54752; alr1080.

Other

ProtoNet

P54752.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 427`	`427`	`Acetylornithine aminotransferase.`	`PRO_0000112714`
`BINDING`	`277 277`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 46140 Da [This is the MW of the unprocessed precursor]

CRC64: 6AF594BB4B3B134E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLQTLIEQA TNPPESGSAA SSPFSTDSFD ASVMSTYGRF PLALERGAGC RVWDTQGKEY 

        70         80         90        100        110        120 
LDFVAGIATC TLGHAHPAMV EAVTRQIQKL HHVSNLYYIP EQGELAQWII QHSCADRVFF 

       130        140        150        160        170        180 
CNSGAEANEA AIKLARKYAH TVLDIEKPII LTANASFHGR TLATITATGQ AKYQKYFDPL 

       190        200        210        220        230        240 
VPGFHYVNYN DISAVEAAIS ELDEGDYRVA AILIEPLQGE GGVRPGDVEY FQKLRQICDD 

       250        260        270        280        290        300 
TGILLMFDEV QVGMGRSGKL WGYEYLGVEP DIFTSAKGLG GGIPIGAMMS KKFCDVFQPG 

       310        320        330        340        350        360 
EHASTFGGNP FACGVALAVC QTLERENILQ NVQDRGEQLR SGLRAIAAKY PHHLTEVRGW 

       370        380        390        400        410        420 
GLINGLELAA DIPLTAADVV KAAINEGLLL VPAGPKVVRF VPPLIVTEAE INTALKLLEK 


ALATVTA

P54752 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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