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Protein

Succinylornithine transaminase

Gene

astC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.1 Publication

Catalytic activityi

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

Cofactori

Pathway: L-arginine degradation via AST pathway

This protein is involved in step 3 of the subpathway that synthesizes L-glutamate and succinate from L-arginine.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Arginine N-succinyltransferase (astA), Arginine N-succinyltransferase (astA)
  2. N-succinylarginine dihydrolase (astB), N-succinylarginine dihydrolase (astB)
  3. Succinylornithine transaminase (astC), Succinylornithine transaminase (astC)
  4. N-succinylglutamate 5-semialdehyde dehydrogenase (astD), N-succinylglutamate 5-semialdehyde dehydrogenase (astD)
  5. Succinylglutamate desuccinylase (astE), Succinylglutamate desuccinylase (astE)
This subpathway is part of the pathway L-arginine degradation via AST pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate and succinate from L-arginine, the pathway L-arginine degradation via AST pathway and in Amino-acid degradation.

GO - Molecular functioni

  • pyridoxal phosphate binding Source: UniProtKB-HAMAP
  • succinylornithine transaminase activity Source: EcoliWiki

GO - Biological processi

  • arginine catabolic process Source: EcoliWiki
  • arginine catabolic process to glutamate Source: UniProtKB-HAMAP
  • arginine catabolic process to succinate Source: EcoCyc
  • ornithine catabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Arginine metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:SUCCORNTRANSAM-MONOMER.
ECOL316407:JW1737-MONOMER.
MetaCyc:SUCCORNTRANSAM-MONOMER.
UniPathwayiUPA00185; UER00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinylornithine transaminase (EC:2.6.1.81)
Short name:
SOAT
Alternative name(s):
Carbon starvation protein C
Succinylornithine aminotransferase
Gene namesi
Name:astC
Synonyms:argM, cstC, ydjW
Ordered Locus Names:b1748, JW1737
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13999. argM.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Succinylornithine transaminasePRO_0000120352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP77581.
PRIDEiP77581.

Interactioni

Protein-protein interaction databases

DIPiDIP-9145N.
IntActiP77581. 2 interactions.
STRINGi511145.b1748.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 137Combined sources
Beta strandi25 – 306Combined sources
Beta strandi32 – 354Combined sources
Beta strandi40 – 456Combined sources
Helixi46 – 494Combined sources
Helixi58 – 6811Combined sources
Helixi81 – 9313Combined sources
Beta strandi97 – 1048Combined sources
Helixi105 – 12319Combined sources
Beta strandi130 – 1345Combined sources
Helixi143 – 1486Combined sources
Helixi152 – 1543Combined sources
Helixi156 – 1583Combined sources
Beta strandi163 – 1686Combined sources
Helixi173 – 1775Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi191 – 1933Combined sources
Turni194 – 1974Combined sources
Beta strandi198 – 2003Combined sources
Helixi203 – 21513Combined sources
Beta strandi219 – 2235Combined sources
Turni225 – 2328Combined sources
Beta strandi233 – 2364Combined sources
Helixi237 – 2415Combined sources
Beta strandi246 – 2505Combined sources
Helixi252 – 2554Combined sources
Beta strandi261 – 2655Combined sources
Helixi267 – 2715Combined sources
Helixi286 – 29914Combined sources
Helixi302 – 32625Combined sources
Beta strandi329 – 3357Combined sources
Beta strandi338 – 3436Combined sources
Turni345 – 3495Combined sources
Helixi351 – 36010Combined sources
Beta strandi366 – 3694Combined sources
Beta strandi372 – 3754Combined sources
Helixi383 – 40119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP77581.
SMRiP77581. Positions 3-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4992.
HOGENOMiHOG000020206.
InParanoidiP77581.
KOiK00840.
OMAiMPEGFIN.
OrthoDBiEOG6QVRHN.
PhylomeDBiP77581.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3.
MF_01173. AstC_aminotrans_3.
InterProiIPR017652. Ac/SucOrn_transaminase_bac.
IPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR026330. SOAT.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77581-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPITRENF DEWMIPVYAP APFIPVRGEG SRLWDQQGKE YIDFAGGIAV
60 70 80 90 100
NALGHAHPEL REALNEQASK FWHTGNGYTN EPVLRLAKKL IDATFADRVF
110 120 130 140 150
FCNSGAEANE AALKLARKFA HDRYGSHKSG IVAFKNAFHG RTLFTVSAGG
160 170 180 190 200
QPAYSQDFAP LPADIRHAAY NDINSASALI DDSTCAVIVE PIQGEGGVVP
210 220 230 240 250
ASNAFLQGLR ELCNRHNALL IFDEVQTGVG RTGELYAYMH YGVTPDLLTT
260 270 280 290 300
AKALGGGFPV GALLATEECA RVMTVGTHGT TYGGNPLASA VAGKVLELIN
310 320 330 340 350
TPEMLNGVKQ RHDWFVERLN TINHRYGLFS EVRGLGLLIG CVLNADYAGQ
360 370 380 390 400
AKQISQEAAK AGVMVLIAGG NVVRFAPALN VSEEEVTTGL DRFAAACEHF

VSRGSS
Length:406
Mass (Da):43,665
Last modified:February 1, 1997 - v1
Checksum:iB18ED13644C21176
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti361 – 3611A → R in AAB51148 (PubMed:9696780).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90416 Genomic DNA. Translation: AAB51148.1.
U00096 Genomic DNA. Translation: AAC74818.1.
AP009048 Genomic DNA. Translation: BAA15539.1.
PIRiD64934.
RefSeqiNP_416262.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74818; AAC74818; b1748.
BAA15539; BAA15539; BAA15539.
GeneIDi946255.
KEGGiecj:Y75_p1723.
eco:b1748.
PATRICi32118805. VBIEscCol129921_1820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90416 Genomic DNA. Translation: AAB51148.1.
U00096 Genomic DNA. Translation: AAC74818.1.
AP009048 Genomic DNA. Translation: BAA15539.1.
PIRiD64934.
RefSeqiNP_416262.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP77581.
SMRiP77581. Positions 3-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9145N.
IntActiP77581. 2 interactions.
STRINGi511145.b1748.

Proteomic databases

PaxDbiP77581.
PRIDEiP77581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74818; AAC74818; b1748.
BAA15539; BAA15539; BAA15539.
GeneIDi946255.
KEGGiecj:Y75_p1723.
eco:b1748.
PATRICi32118805. VBIEscCol129921_1820.

Organism-specific databases

EchoBASEiEB3755.
EcoGeneiEG13999. argM.

Phylogenomic databases

eggNOGiCOG4992.
HOGENOMiHOG000020206.
InParanoidiP77581.
KOiK00840.
OMAiMPEGFIN.
OrthoDBiEOG6QVRHN.
PhylomeDBiP77581.

Enzyme and pathway databases

UniPathwayiUPA00185; UER00281.
BioCyciEcoCyc:SUCCORNTRANSAM-MONOMER.
ECOL316407:JW1737-MONOMER.
MetaCyc:SUCCORNTRANSAM-MONOMER.

Miscellaneous databases

PROiP77581.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_01107. ArgD_aminotrans_3.
MF_01173. AstC_aminotrans_3.
InterProiIPR017652. Ac/SucOrn_transaminase_bac.
IPR004636. AcOrn/SuccOrn_fam.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR026330. SOAT.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiASTC_ECOLI
AccessioniPrimary (citable) accession number: P77581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.