ID   ASTA_YERE8              Reviewed;         345 AA.
AC   A1JS43;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=YE2468;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12511.1; -; Genomic_DNA.
DR   RefSeq; WP_005169035.1; NC_008800.1.
DR   RefSeq; YP_001006675.1; NC_008800.1.
DR   AlphaFoldDB; A1JS43; -.
DR   SMR; A1JS43; -.
DR   STRING; 393305.YE2468; -.
DR   EnsemblBacteria; CAL12511; CAL12511; YE2468.
DR   KEGG; yen:YE2468; -.
DR   PATRIC; fig|393305.7.peg.2619; -.
DR   eggNOG; COG3138; Bacteria.
DR   HOGENOM; CLU_057655_0_0_6; -.
DR   OMA; PEENRSW; -.
DR   UniPathway; UPA00185; UER00279.
DR   Proteomes; UP000000642; 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..345
FT                   /note="Arginine N-succinyltransferase"
FT                   /id="PRO_1000065711"
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   345 AA;  38669 MW;  CEA62E47F78E18A5 CRC64;
     MMRVRPVERR DLADILELAG KTGVGMTSLP QNEQHLAARI ERALNTWQGS LAVGEQGYLF
     VLEDTEREKV VGVSAIEVAV GMNDPWYNFR VGTLVHASKT LNVYKSVPTL FLSNDHTGYS
     ELCTLFLDPE YRKDKNGPFL SKVRFLFIAA FRQHFSRKLI AEMRGYTDEQ GRSPFWENVG
     RHFFSIEFAK ADYLSGTGQK AFIAELMPKH PLYVDFLAEE ARAVIGQVHP HTAPARAVLE
     TEGLQYQGYV DIFDGGPTLE ANTDEVRAVR DSSQRKVVID DIDIDPSGSA YLVANDRYQE
     FRSILINTHL SDEFLHLTPD NAAALGVVAG DVVRIISLFA PETKK