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B6IBG8 (ASTC_ECOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinylornithine transaminase

EC=2.6.1.81
Alternative name(s):
Succinylornithine aminotransferase
Gene names
Name:astC
Synonyms:argM
Ordered Locus Names:ECSE_1918
OrganismEscherichia coli (strain SE11) [Complete proteome] [HAMAP]
Taxonomic identifier409438 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase By similarity. HAMAP MF_01173

Catalytic activity

N(2)-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01173

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_01173

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. HAMAP MF_01173

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.

Ontologies

Keywords
   Biological processArginine metabolism
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

succinylornithine transaminase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Succinylornithine transaminase HAMAP MF_01173
PRO_1000164386

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6IBG8 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: B18ED13644C21176

FASTA40643,665
        10         20         30         40         50         60 
MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV NALGHAHPEL 

        70         80         90        100        110        120 
REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF FCNSGAEANE AALKLARKFA 

       130        140        150        160        170        180 
HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG QPAYSQDFAP LPADIRHAAY NDINSASALI 

       190        200        210        220        230        240 
DDSTCAVIVE PIQGEGGVVP ASNAFLQGLR ELCNRHNALL IFDEVQTGVG RTGELYAYMH 

       250        260        270        280        290        300 
YGVTPDLLTT AKALGGGFPV GALLATEECA RVMTVGTHGT TYGGNPLASA VAGKVLELIN 

       310        320        330        340        350        360 
TPEMLNGVKQ RHDWFVERLN TINHRYGLFS EVRGLGLLIG CVLNADYAGQ AKQISQEAAK 

       370        380        390        400 
AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF VSRGSS 

« Hide

References

[1]"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SE11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009240 Genomic DNA. Translation: BAG77442.1.
RefSeqYP_002293193.1. NC_011415.1.

3D structure databases

ProteinModelPortalB6IBG8.
SMRB6IBG8. Positions 15-396.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6IBG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000110439; EBESCP00000103962; EBESCG00000106669.
GeneID7000296.
GenomeReviewsGene locus ECSE_1918 in contig AP009240_GR.
KEGGecy:ECSE_1918.
PATRIC18422338. VBIEscCol83070_2064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010246.
HOGENOMHBG725944.
OMAPERFRIV.
ProtClustDBPRK12381.

Enzyme and pathway databases

BioCycECOL409438:ECSE_1918-MONOMER.

Family and domain databases

HAMAPMF_01173. AstC_aminotrans_3.
[Tree]
InterProIPR017652. Ac/SuccinylOrn_transaminase.
IPR004636. AcOrn/SuccinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00840.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR03246. Arg_catab_astC. 1 hit.
TIGR00707. ArgD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASTC_ECOSE
AccessionPrimary (citable) accession number: B6IBG8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families