ID   ASTA_ECO57              Reviewed;         344 AA.
AC   P0AE38; P76218;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Arginine N-succinyltransferase;
DE            Short=AST;
DE            EC=2.3.1.109;
DE   AltName: Full=AOST;
GN   Name=astA; OrderedLocusNames=Z2779, ECs2453;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to
CC       produce N(2)-succinylarginine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + L-arginine = CoA + N(2)-
CC       succinyl-L-arginine.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 1/5.
CC   -!- SIMILARITY: Belongs to the arginine N-succinyltransferase family.
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DR   EMBL; AE005174; AAG56733.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35876.1; -; Genomic_DNA.
DR   PIR; A85784; A85784.
DR   PIR; E90935; E90935.
DR   RefSeq; NP_288180.1; -.
DR   RefSeq; NP_310480.1; -.
DR   GeneID; 913079; -.
DR   GeneID; 961718; -.
DR   GenomeReviews; AE005174_GR; Z2779.
DR   GenomeReviews; BA000007_GR; ECs2453.
DR   KEGG; ece:Z2779; -.
DR   KEGG; ecs:ECs2453; -.
DR   HOGENOM; P0AE38; -.
DR   OMA; P0AE38; TLFLAND.
DR   BioCyc; ECOL83334:ECS2453-MON; -.
DR   GO; GO:0008791; F:arginine N-succinyltransferase activity; IEA:HAMAP.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP.
DR   HAMAP; MF_01171; -; 1.
DR   InterPro; IPR007041; Arg_N-succinylTrfase_Ast/AOST.
DR   InterPro; IPR017650; Arginine_N-succinylTrfase_AstA.
DR   Pfam; PF04958; AstA; 1.
DR   TIGRFAMs; TIGR03243; arg_catab_AOST; 1.
DR   TIGRFAMs; TIGR03244; arg_catab_AstA; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Arginine metabolism; Complete proteome; Transferase.
FT   CHAIN         1    344       Arginine N-succinyltransferase.
FT                                /FTId=PRO_0000064713.
FT   ACT_SITE    229    229       Proton donor (Potential).
FT   BINDING     125    125       Succinyl-CoA; via amide nitrogen
FT                                (Potential).
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
//