ID   ASTA_PHOLL              Reviewed;         343 AA.
AC   Q7N2G8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=plu3109;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15483.1; -; Genomic_DNA.
DR   RefSeq; WP_011147325.1; NC_005126.1.
DR   AlphaFoldDB; Q7N2G8; -.
DR   SMR; Q7N2G8; -.
DR   STRING; 243265.plu3109; -.
DR   EnsemblBacteria; CAE15483; CAE15483; plu3109.
DR   GeneID; 24170072; -.
DR   KEGG; plu:plu3109; -.
DR   eggNOG; COG3138; Bacteria.
DR   HOGENOM; CLU_057655_0_0_6; -.
DR   OMA; PEENRSW; -.
DR   OrthoDB; 972674at2; -.
DR   BioCyc; PLUM243265:PLU_RS15480-MON; -.
DR   UniPathway; UPA00185; UER00279.
DR   Proteomes; UP000002514; 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; Reference proteome; Transferase.
FT   CHAIN           1..343
FT                   /note="Arginine N-succinyltransferase"
FT                   /id="PRO_0000262326"
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   343 AA;  37995 MW;  CB13861B865CFA62 CRC64;
     MMLFRAVRHS DLNGVQSLSQ RAGIGLTSFP NNLDQLRSRI ARSVDTFDGK LARAQQGFLF
     VLEDTSANRV AGVSAIEVAV GLEEPFYNFR VQKTIRSSRE LGIYKSIEAL TLEQDQTGNS
     ELCTLFLDPE YQKGRNGTFL SKARFLFIAA FRDIFSKTIF AEMRGVADEQ GNSPFWNSLG
     QHFFGIPFSQ ADYLTGIGSK TFIAELMPLH PIYISLLSAE AQKVIGQVHE KTVPARAILE
     KEGLIYQGHI DIFDGGALLQ AEIDRIRAVK ESRLVSVSKA ESVTRDDGVP CIVANQQFSE
     FRALLLNVVC DSNELFLTAA EMGALQVSDG DQVRLVSLFP KEN