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P77581 (ASTC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinylornithine transaminase

Short name=SOAT
EC=2.6.1.81
Alternative name(s):
Carbon starvation protein C
Succinylornithine aminotransferase
Gene names
Name:astC
Synonyms:argM, cstC, ydjW
Ordered Locus Names:b1748, JW1737
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.5

Catalytic activity

N(2)-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP-Rule MF_01107

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. HAMAP-Rule MF_01107

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1125336,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Succinylornithine transaminase HAMAP-Rule MF_01107
PRO_0000120352

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3611A → R in AAB51148. Ref.1

Secondary structure

..................................................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77581 [UniParc].

Last modified February 1, 1997. 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

« Hide 'large scale' references
[1]"The Escherichia coli starvation gene cstC is involved in amino acid catabolism."
Fraley C.D., Kim J.H., McCann M.P., Matin A.
J. Bacteriol. 180:4287-4290(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli."
Schneider B.L., Kiupakis A.K., Reitzer L.J.
J. Bacteriol. 180:4278-4286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-21 AND 295-309, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90416 Genomic DNA. Translation: AAB51148.1.
U00096 Genomic DNA. Translation: AAC74818.1.
AP009048 Genomic DNA. Translation: BAA15539.1.
PIRD64934.
RefSeqNP_416262.1. NC_000913.3.
YP_490009.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ADBX-ray2.20A/B/C/D1-406[»]
4ADCX-ray2.30A/B/C/D1-406[»]
4ADDX-ray2.45A/B/C/D1-406[»]
4ADEX-ray2.75A/B1-406[»]
ProteinModelPortalP77581.
SMRP77581. Positions 3-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9145N.
IntActP77581. 2 interactions.
STRING511145.b1748.

Proteomic databases

PaxDbP77581.
PRIDEP77581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74818; AAC74818; b1748.
BAA15539; BAA15539; BAA15539.
GeneID12934011.
946255.
KEGGecj:Y75_p1723.
eco:b1748.
PATRIC32118805. VBIEscCol129921_1820.

Organism-specific databases

EchoBASEEB3755.
EcoGeneEG13999. argM.

Phylogenomic databases

eggNOGCOG4992.
HOGENOMHOG000020206.
KOK00840.
OMARTKMPKE.
OrthoDBEOG6QVRHN.
PhylomeDBP77581.
ProtClustDBPRK12381.

Enzyme and pathway databases

BioCycEcoCyc:SUCCORNTRANSAM-MONOMER.
ECOL316407:JW1737-MONOMER.
MetaCyc:SUCCORNTRANSAM-MONOMER.
UniPathwayUPA00185; UER00281.

Gene expression databases

GenevestigatorP77581.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_01107. ArgD_aminotrans_3.
MF_01173. AstC_aminotrans_3.
InterProIPR017652. Ac/SucOrn_transaminase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR026330. SOAT.
IPR004636. Trfase_AcOrn/SuccOrn_fam.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP77581.

Entry information

Entry nameASTC_ECOLI
AccessionPrimary (citable) accession number: P77581
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene