Succinylornithine transaminase - Escherichia coli (strain K12)

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P77581 (ASTC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Protein existence	Evidence 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_01173
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_01173
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.

Ontologies

Keywords
Biological process	Arginine metabolism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process to succinate Inferred from mutant phenotype Ref.5. Source: EcoCyc ornithine catabolic process Inferred from mutant phenotype Ref.1. Source: EcoCyc
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro succinylornithine transaminase activity Inferred from direct assay Ref.5. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1125336,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 406

406

Succinylornithine transaminase HAMAP-Rule MF_01173

PRO_0000120352

Amino acid modifications

Modified residue

252

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

361

A → R in AAB51148. Ref.1

Secondary structure

406

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P77581 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B18ED13644C21176
Show »

FASTA

406

43,665

        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' referencesShow '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. 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 277:1453-1474(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.

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.

PIR

D64934.

RefSeq

NP_416262.1. NC_000913.2.
YP_490009.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4ADB	X-ray	2.20	A/B/C/D	1-406	[»]
4ADC	X-ray	2.30	A/B/C/D	1-406	[»]
4ADD	X-ray	2.45	A/B/C/D	1-406	[»]
4ADE	X-ray	2.75	A/B	1-406	[»]

ProteinModelPortal

P77581.

SMR

P77581. Positions 15-396.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9145N.

IntAct

P77581. 1 interaction.

STRING

511145.b1748.

Proteomic databases

PaxDb

P77581.

PRIDE

P77581.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74818; AAC74818; b1748.
BAA15539; BAA15539; BAA15539.

GeneID

12934011.
946255.

KEGG

ecj:Y75_p1723.
eco:b1748.

PATRIC

32118805. VBIEscCol129921_1820.

Organism-specific databases

EchoBASE

EB3755.

EcoGene

EG13999. argM.

Phylogenomic databases

eggNOG

COG4992.

HOGENOM

HOG000020206.

K00840.

OMA

KIIEDAH.

ProtClustDB

PRK12381.

Enzyme and pathway databases

BioCyc

EcoCyc:SUCCORNTRANSAM-MONOMER.
ECOL316407:JW1737-MONOMER.
MetaCyc:SUCCORNTRANSAM-MONOMER.

UniPathway

UPA00185; UER00281.

Gene expression databases

Genevestigator

P77581.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.

HAMAP

MF_01173. AstC_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.
IPR026330. SOAT.
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

ASTC_ECOLI

Accession

Primary (citable) accession number: P77581

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents