ASTA_ECOLC
ID ASTA_ECOLC Reviewed; 344 AA.
AC B1IPI3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=EcolC_1885;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000946; ACA77533.1; -; Genomic_DNA.
DR RefSeq; WP_000989419.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IPI3; -.
DR SMR; B1IPI3; -.
DR KEGG; ecl:EcolC_1885; -.
DR HOGENOM; CLU_057655_0_0_6; -.
DR OMA; RFFSMEF; -.
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..344
FT /note="Arginine N-succinyltransferase"
FT /id="PRO_1000085390"
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; 38456 MW; 89C7BB412A880BEF CRC64;
MMVIRPVERS 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 QPAQGDFPAC LVANENYHHF
RVVLVRTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA
