ID   ASTA_ESCF3              Reviewed;         344 AA.
AC   B7LQ45;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=EFER_1318;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ88842.1; -; Genomic_DNA.
DR   RefSeq; WP_000989454.1; NC_011740.1.
DR   AlphaFoldDB; B7LQ45; -.
DR   SMR; B7LQ45; -.
DR   EnsemblBacteria; CAQ88842; CAQ88842; EFER_1318.
DR   GeneID; 60900067; -.
DR   KEGG; efe:EFER_1318; -.
DR   HOGENOM; CLU_057655_0_0_6; -.
DR   OMA; RFFSMEF; -.
DR   OrthoDB; 972674at2; -.
DR   BioCyc; EFER585054:EFER_RS06670-MON; -.
DR   UniPathway; UPA00185; UER00279.
DR   Proteomes; UP000000745; 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_1000137983"
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;  38484 MW;  1FD3F87678BC7912 CRC64;
     MMVIRPVERT DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF
     VLEDSETGTV AGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS
     ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG
     KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE
     KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGEFPAC LVANENYHHF
     RVVLVRTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA