ASTA_ECOLI
ID ASTA_ECOLI Reviewed; 344 AA.
AC P0AE37; P76218; Q2MB39;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Arginine N-succinyltransferase;
DE Short=AST;
DE EC=2.3.1.109;
DE AltName: Full=AOST;
GN Name=astA; Synonyms=ydjV; OrderedLocusNames=b1747, JW1736;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION.
RX PubMed=9696779; DOI=10.1128/jb.180.16.4278-4286.1998;
RA Schneider B.L., Kiupakis A.K., Reitzer L.J.;
RT "Arginine catabolism and the arginine succinyltransferase pathway in
RT Escherichia coli.";
RL J. Bacteriol. 180:4278-4286(1998).
RN [4]
RP INDUCTION.
RX PubMed=12003934; DOI=10.1128/jb.184.11.2940-2950.2002;
RA Kiupakis A.K., Reitzer L.;
RT "ArgR-independent induction and ArgR-dependent superinduction of the
RT astCADBE operon in Escherichia coli.";
RL J. Bacteriol. 184:2940-2950(2002).
RN [5]
RP 3D-STRUCTURE MODELING, AND REACTION MECHANISM.
RX PubMed=14675764; DOI=10.1016/s0014-5793(03)01314-0;
RA Shirai H., Mizuguchi K.;
RT "Prediction of the structure and function of AstA and AstB, the first two
RT enzymes of the arginine succinyltransferase pathway of arginine
RT catabolism.";
RL FEBS Lett. 555:505-510(2003).
CC -!- FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce
CC N(2)-succinylarginine. {ECO:0000269|PubMed:9696779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-
CC arginine; Xref=Rhea:RHEA:15185, ChEBI:CHEBI:15378, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:58241;
CC EC=2.3.1.109;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 1/5.
CC -!- INDUCTION: By nitrogen starvation, and arginine. Induced at stationary
CC phase by sigma S. {ECO:0000269|PubMed:12003934}.
CC -!- SIMILARITY: Belongs to the arginine N-succinyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74817.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76517.1; -; Genomic_DNA.
DR PIR; C64934; C64934.
DR RefSeq; NP_416261.1; NC_000913.3.
DR RefSeq; WP_000989419.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0AE37; -.
DR SMR; P0AE37; -.
DR BioGRID; 4262235; 8.
DR IntAct; P0AE37; 6.
DR STRING; 511145.b1747; -.
DR jPOST; P0AE37; -.
DR PaxDb; P0AE37; -.
DR PRIDE; P0AE37; -.
DR EnsemblBacteria; AAC74817; AAC74817; b1747.
DR EnsemblBacteria; BAE76517; BAE76517; BAE76517.
DR GeneID; 946261; -.
DR KEGG; ecj:JW1736; -.
DR KEGG; eco:b1747; -.
DR PATRIC; fig|1411691.4.peg.509; -.
DR EchoBASE; EB3754; -.
DR eggNOG; COG3138; Bacteria.
DR HOGENOM; CLU_057655_0_0_6; -.
DR InParanoid; P0AE37; -.
DR OMA; RFFSMEF; -.
DR PhylomeDB; P0AE37; -.
DR BioCyc; EcoCyc:ARGSUCCTRAN-MON; -.
DR BioCyc; MetaCyc:ARGSUCCTRAN-MON; -.
DR UniPathway; UPA00185; UER00279.
DR PRO; PR:P0AE37; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008791; F:arginine N-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01171; AstA; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR007041; Arg_succinylTrfase_AstA/AruG.
DR InterPro; IPR017650; Arginine_N-succinylTrfase.
DR Pfam; PF04958; AstA; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03243; arg_catab_AOST; 1.
DR TIGRFAMs; TIGR03244; arg_catab_AstA; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Arginine metabolism; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..344
FT /note="Arginine N-succinyltransferase"
FT /id="PRO_0000064712"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 125
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255"
SQ SEQUENCE 344 AA; 38456 MW; 89C7BB412A880BEF CRC64;
MMVIRPVERS DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF
VLEDSETGTV AGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS
ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG
KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE
KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGDFPAC LVANENYHHF
RVVLVRTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA
