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A7ZML6 (ASTC_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:EcE24377A_1970
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [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_1000164373

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZML6 [UniParc].

Last modified October 23, 2007. 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]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV19758.1.
RefSeqYP_001463045.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZML6.
SMRA7ZML6. Positions 15-396.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZML6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000022027; EBESCP00000021089; EBESCG00000021081.
GeneID5588995.
GenomeReviewsGene locus EcE24377A_1970 in contig CP000800_GR.
KEGGecw:EcE24377A_1970.
PATRIC18293186. VBIEscCol31211_2246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4992.
GeneTreeEBGT00050000010246.
HOGENOMHBG725944.
OMAPERFRIV.
ProtClustDBPRK12381.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_1970-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_ECO24
AccessionPrimary (citable) accession number: A7ZML6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 33 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