ID   ASTA_SHIB3              Reviewed;         344 AA.
AC   B2U3C9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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};
GN   OrderedLocusNames=SbBS512_E1994;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD09891.1; -; Genomic_DNA.
DR   RefSeq; WP_000989403.1; NC_010658.1.
DR   AlphaFoldDB; B2U3C9; -.
DR   SMR; B2U3C9; -.
DR   STRING; 344609.SbBS512_E1994; -.
DR   EnsemblBacteria; ACD09891; ACD09891; SbBS512_E1994.
DR   KEGG; sbc:SbBS512_E1994; -.
DR   HOGENOM; CLU_057655_0_0_6; -.
DR   OMA; RFFSMEF; -.
DR   UniPathway; UPA00185; UER00279.
DR   Proteomes; UP000001030; 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_1000137991"
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;  38386 MW;  0B4B5C313357AFB4 CRC64;
     MMVIRPVERS DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF
     VLEDSETGTV AGICAIEVAV GLNDPWHNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS
     ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG
     KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE
     KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGDFPAC LVANENYHHF
     RVVLARTDPA TERLILTAAQ LDALKCHAGE RVRLVRLCAV EKTA