ID   ASTA_YERPP              Reviewed;         350 AA.
AC   A4TJU6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=YPDSF_1160;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pestoides F;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-2007) 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; CP000668; ABP39558.1; -; Genomic_DNA.
DR   RefSeq; WP_002212031.1; NZ_CP009715.1.
DR   AlphaFoldDB; A4TJU6; -.
DR   SMR; A4TJU6; -.
DR   KEGG; ypp:YPDSF_1160; -.
DR   PATRIC; fig|386656.14.peg.2665; -.
DR   OMA; PEENRSW; -.
DR   UniPathway; UPA00185; UER00279.
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..350
FT                   /note="Arginine N-succinyltransferase"
FT                   /id="PRO_1000065712"
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   350 AA;  39468 MW;  1F3C02A1B04C92BD CRC64;
     MMKVRPVERR DLADIFELAG KTGVGMTSLP QNEQHLAARI ERALNTWQGS LDPGEQGYLF
     VLEDSEQQKV VGVSAIEVAV GLNDPWYNFR VGTLVHASKA LNVYKSVPTL FLSNDHTGYS
     ELCTLFLDPD YRKDKNGPFL SKVRFLFIAA FRQYFSRKVI AEMRGYTDEQ GRSPFWESVG
     RHFFSIEFAK ADYLSGTGQK AFIAELMPKH PLYVDFLAEE ARAVIGQVHP HTAPARAVLE
     TEGLQYQGYV DIFDGGPTLE ANTDDVRVVR DSSKRTVVIK DYDIEDYDID PNGRLYLVAN
     DHYHHFRAIL MNTHLSDERL RLTPESAEAL GVAAGDSVRI VSLFAPETKR