P0AE37 (ASTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine N-succinyltransferase
Short name=AST
EC=2.3.1.109

Alternative name(s):
AOST

Gene names

Name:	astA
Synonyms:	ydjV
Ordered Locus Names:	b1747, JW1736

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. Ref.3
Catalytic activity	Succinyl-CoA + L-arginine = CoA + N(2)-succinyl-L-arginine. HAMAP-Rule MF_01171
Pathway	Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. HAMAP-Rule MF_01171
Induction	By nitrogen starvation, and arginine. Induced at stationary phase by sigma S. Ref.4
Sequence similarities	Belongs to the arginine N-succinyltransferase family.

Ontologies

Keywords
Biological process	Arginine metabolism Stress response
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process to glutamate Inferred from electronic annotation. Source: HAMAP arginine catabolic process to succinate Inferred from electronic annotation. Source: UniProtKB-UniPathway response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	arginine N-succinyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Arginine N-succinyltransferase HAMAP-Rule MF_01171		PRO_0000064712
Sites
	Active site	229	1	Proton donor Potential
	Binding site	125	1	Succinyl-CoA; via amide nitrogen Potential

Sequences

	Sequence		Length	Mass (Da)
	P0AE37 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 89C7BB412A880BEF	FASTA	344	38,456
	10 20 30 40 50 60 MMVIRPVERS DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF 70 80 90 100 110 120 VLEDSETGTV AGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS 130 140 150 160 170 180 ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG 190 200 210 220 230 240 KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE 250 260 270 280 290 300 KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGDFPAC LVANENYHHF 310 320 330 340 RVVLVRTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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: FUNCTION.
[4]	"ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." Kiupakis A.K., Reitzer L. J. Bacteriol. 184:2940-2950(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[5]	"Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism." Shirai H., Mizuguchi K. FEBS Lett. 555:505-510(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, REACTION MECHANISM.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74817.1. AP009048 Genomic DNA. Translation: BAE76517.1.
PIR	C64934.
RefSeq	NP_416261.1. NC_000913.2. YP_490008.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AE37.
SMR	P0AE37. Positions 1-335.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AE37. 6 interactions.
STRING	511145.b1747.
Proteomic databases
PRIDE	P0AE37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74817; AAC74817; b1747. BAE76517; BAE76517; BAE76517.
GeneID	12933241. 946261.
KEGG	ecj:Y75_p1722. eco:b1747.
PATRIC	32118803. VBIEscCol129921_1819.
Organism-specific databases
EchoBASE	EB3754.
EcoGene	EG13998. astA.
Phylogenomic databases
eggNOG	COG3138.
HOGENOM	HOG000258231.
KO	K00673.
OMA	AGPAIEC.
ProtClustDB	PRK10456.
Enzyme and pathway databases
BioCyc	EcoCyc:ARGSUCCTRAN-MONOMER. ECOL316407:JW1736-MONOMER. MetaCyc:ARGSUCCTRAN-MONOMER.
UniPathway	UPA00185; UER00279.
Gene expression databases
Genevestigator	P0AE37.
Family and domain databases
Gene3D	2.40.40.20. 1 hit. 3.40.630.30. 2 hits.
HAMAP	MF_01171. AstA.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR007041. Arg_N-succinylTrfase_Ast/AOST. IPR017650. Arginine_N-succinylTrfase_AstA. IPR009010. Asp_de-COase-like_dom. [Graphical view]
Pfam	PF04958. AstA. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMs	TIGR03243. arg_catab_AOST. 1 hit. TIGR03244. arg_catab_AstA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ASTA_ECOLI

Accession

Primary (citable) accession number: P0AE37
Secondary accession number(s): P76218, Q2MB39

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program