ID   ASTA_SALTY              Reviewed;         344 AA.
AC   Q8ZPV1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=Arginine N-succinyltransferase;
DE            Short=AST;
DE            EC=2.3.1.109;
DE   AltName: Full=AOST;
GN   Name=astA; OrderedLocusNames=STM1304;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   INDUCTION.
RX   MEDLINE=99173922; PubMed=10074092;
RA   Lu C.-D., Abdelal A.T.;
RT   "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT   arginine succinyltransferase pathway in Salmonella typhimurium.";
RL   J. Bacteriol. 181:1934-1938(1999).
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   -!- INDUCTION: By nitrogen and carbon starvation, and arginine, via
CC       the argR and crp transcriptional regulators.
CC   -!- SIMILARITY: Belongs to the arginine N-succinyltransferase family.
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DR   EMBL; AE008756; AAL20229.1; -; Genomic_DNA.
DR   RefSeq; NP_460270.1; -.
DR   GeneID; 1252822; -.
DR   GenomeReviews; AE006468_GR; STM1304.
DR   KEGG; stm:STM1304; -.
DR   HOGENOM; Q8ZPV1; -.
DR   OMA; Q8ZPV1; TLFLAND.
DR   BioCyc; STYP99287:STM1304-MON; -.
DR   BRENDA; 2.3.1.109; 2.
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   2: Evidence at transcript level;
KW   Acyltransferase; Arginine metabolism; Complete proteome; Transferase.
FT   CHAIN         1    344       Arginine N-succinyltransferase.
FT                                /FTId=PRO_0000262329.
FT   ACT_SITE    229    229       Proton donor (Potential).
FT   BINDING     125    125       Succinyl-CoA; via amide nitrogen
FT                                (Potential).
SQ   SEQUENCE   344 AA;  38278 MW;  52B3BA6BB43B8767 CRC64;
     MRVIRPVEHA DIAALMQLAG KTGGGLTSLP ANEATLAARI ERALKTWSGE LPKGEQGYVF
     VLEDSETGEV GGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS
     ELCTLFLDPE WRKEGNGYLL SKSRFMFMAA FRDKFNEKVV AEMRGVIDEH GYSPFWQSLG
     KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSEE AQAVIGEVHP QTAPARAVLE
     KEGFRYRHYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAPGDYPAC LVANENYHHF
     RAALVRADPQ TSRLVLTAAQ LDALKCRAGD HVRLVRLCAE EKTV
//