Acetylornithine/succinyldiaminopimelate aminotransferase

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D5AYN1 (D5AYN1_YERPZ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 25. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP-Rule MF_01107
Short name=ACOAT HAMAP-Rule MF_01107
Short name=DapATase HAMAP-Rule MF_01107
Short name=Succinyldiaminopimelate transferase HAMAP-Rule MF_01107
EC=2.6.1.11 HAMAP-Rule MF_01107
EC=2.6.1.17 HAMAP-Rule MF_01107

Gene names

Name:	argD HAMAP-Rule MF_01107
Synonyms:	dapC HAMAP-Rule MF_01107
Ordered Locus Names:	YPZ3_0149 EMBL ADE63059.1

Organism

Yersinia pestis (strain Z176003) [Complete proteome] [HAMAP] EMBL ADE63059.1

Taxonomic identifier

637386 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia ›

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis HAMAP-Rule MF_01107 Lysine biosynthesis HAMAP-Rule MF_01107
Cellular component	Cytoplasm HAMAP-Rule MF_01107
Ligand	Pyridoxal phosphate SAAS SAAS017652 HAMAP-Rule MF_01107
Molecular function	Aminotransferase SAAS SAAS017652 HAMAP-Rule MF_01107 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: UniProtKB-UniPathway
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

225 – 228

Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site

140

Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107

Binding site

143

N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107

Binding site

282

N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107

Binding site

283

Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue

254

N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence

Length

Mass (Da)

Tools

D5AYN1 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 2836624C4D6D517E
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FASTA

405

43,331

        10         20         30         40         50         60 
MTDKLAVNRN TFDQVILPVY APAQFIPVKG KGSRVWDQQG TEYIDFAGGI AVTALGHCHP 

        70         80         90        100        110        120 
ALVSALHQQG ETLWHTSNVF TNEPALRLAQ KLIAATFADR VFFANSGAEA NEAAFKLARH 

       130        140        150        160        170        180 
YAIERHSPYK TKIIAFHNAF HGRTLFTVSV GGQPKYSDGF GPKPADIIHV PFNDLAAVKA 

       190        200        210        220        230        240 
VMDDHTCAVV LEPIQGEGGI TSATPEFLQG VRALCDQHNA LLVFDEVQSG MGRSGKLFSY 

       250        260        270        280        290        300 
MHYGVTPDIL TTAKALGGGF PISAMLTTEE IASVMTVGTH GTTYGGNPLA CAVAEAALDV 

       310        320        330        340        350        360 
INTPEVLNGI EQRHGLFVQA LQSINSKYDV FSDIRGMGLL IGAELTAKYR GQAREFLAAA 

       370        380        390        400 
AANGLMILNA GPDVLRLAPS LVIELEDIQQ GMARLEKAMA SVIKG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Yersinia pestis from new plague natural foci in China." Hai R., Yu D., Xia L., Zhu X., Liang Y., Shen X., Zhang E., Zhang H. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Z176003.
[2]	"Complete genome sequences of Yersinia pestis from natural foci in China." Shen X., Wang Q., Xia L., Zhu X., Zhang Z., Liang Y., Cai H., Zhang E., Wei J., Chen C., Song Z., Zhang H., Yu D., Hai R. J. Bacteriol. 192:3551-3552(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z176003 EMBL ADE63059.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001593 Genomic DNA. Translation: ADE63059.1.
RefSeq	YP_003566321.1. NC_014029.1.
3D structure databases
ProteinModelPortal	D5AYN1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADE63059; ADE63059; YPZ3_0149.
GeneID	8990045.
KEGG	ypz:YPZ3_0149.
PATRIC	35467361. VBIYerPes97410_0416.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000020206.
KO	K00821.
OMA	MHYGITP.
Enzyme and pathway databases
UniPathway	UPA00034; UER00020. UPA00068; UER00109.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_01107. ArgD_aminotrans_3.
InterPro	IPR017652. Ac/SucOrn_transaminase_bac. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. IPR004636. Trfase_AcOrn/SuccOrn_fam. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit. PTHR11986:SF19. PTHR11986:SF19. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
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

D5AYN1_YERPZ

Accession

Primary (citable) accession number: D5AYN1

Entry history

Integrated into UniProtKB/TrEMBL:	June 15, 2010
Last sequence update:	June 15, 2010
Last modified:	May 1, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information