ID   ASTA_SALA4              Reviewed;         344 AA.
AC   B5F845;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Arginine N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_01171};
DE            Short=AST {ECO:0000255|HAMAP-Rule:MF_01171};
DE            EC=2.3.1.109 {ECO:0000255|HAMAP-Rule:MF_01171};
DE   AltName: Full=AOST {ECO:0000255|HAMAP-Rule:MF_01171};
GN   Name=astA {ECO:0000255|HAMAP-Rule:MF_01171}; OrderedLocusNames=SeAg_B1869;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce
CC       N(2)-succinylarginine. {ECO:0000255|HAMAP-Rule:MF_01171}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01171};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 1/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01171}.
CC   -!- SIMILARITY: Belongs to the arginine N-succinyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01171}.
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DR   EMBL; CP001138; ACH52941.1; -; Genomic_DNA.
DR   RefSeq; WP_001263885.1; NC_011149.1.
DR   AlphaFoldDB; B5F845; -.
DR   SMR; B5F845; -.
DR   EnsemblBacteria; ACH52941; ACH52941; SeAg_B1869.
DR   KEGG; sea:SeAg_B1869; -.
DR   HOGENOM; CLU_057655_0_0_6; -.
DR   OMA; RFFSMEF; -.
DR   UniPathway; UPA00185; UER00279.
DR   Proteomes; UP000008819; 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   3: Inferred from homology;
KW   Acyltransferase; Arginine metabolism; Transferase.
FT   CHAIN           1..344
FT                   /note="Arginine N-succinyltransferase"
FT                   /id="PRO_1000137984"
FT   ACT_SITE        229
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01171"
FT   BINDING         125
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01171"
SQ   SEQUENCE   344 AA;  38336 MW;  A27C86690C990CF7 CRC64;
     MRVIRPVEHA DIAALMQLAG KTGGGLTSLP ANEATLAARI ERALKTWSDE 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