ID ASTA_PSEAE Reviewed; 338 AA. AC P80357; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 02-SEP-2026, entry version 145. DE RecName: Full=Arginine N-succinyltransferase subunit alpha; DE Short=ARUAI; DE EC=2.3.1.109; DE AltName: Full=AOST; DE Short=AST; GN Name=astA; Synonyms=aruF; OrderedLocusNames=PA0896; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=9393691; DOI=10.1128/jb.179.23.7280-7290.1997; RA Itoh Y.; RT "Cloning and characterization of the aru genes encoding enzymes of the RT catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa."; RL J. Bacteriol. 179:7280-7290(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [3] RP PROTEIN SEQUENCE OF 1-11. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=7523119; DOI=10.1111/j.1432-1033.1994.00853.x; RA Tricot C., Vander Wauven C., Wattiez R., Falmagne P., Stalon V.; RT "Purification and properties of a succinyltransferase from Pseudomonas RT aeruginosa specific for both arginine and ornithine."; RL Eur. J. Biochem. 224:853-861(1994). CC -!- FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce CC N(2)-succinylarginine. Also acts on L-ornithine. CC -!- CATALYTIC ACTIVITY: CC Reaction=succinyl-CoA + L-arginine = N(2)-succinyl-L-arginine + CoA + CC H(+); 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; CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST CC pathway; L-glutamate and succinate from L-arginine: step 1/5. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family. CC {ECO:0000305}. 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; AF011922; AAC46010.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04285.1; -; Genomic_DNA. DR PIR; A83533; A83533. DR RefSeq; NP_249587.1; NC_002516.2. DR RefSeq; WP_003085950.1; NC_002516.2. DR PDB; 1YLE; X-ray; 1.70 A; A=1-338. DR AlphaFoldDB; P80357; -. DR SMR; P80357; -. DR STRING; 208964.PA0896; -. DR DrugBank; DB01942; Formic acid. DR PaxDb; 208964-PA0896; -. DR DNASU; 879437; -. DR GeneID; 77222538; -. DR GeneID; 879437; -. DR KEGG; pae:PA0896; -. DR PATRIC; fig|208964.12.peg.931; -. DR PseudoCAP; PA0896; -. DR HOGENOM; CLU_057655_0_0_6; -. DR InParanoid; P80357; -. DR OrthoDB; 21121at2; -. DR PhylomeDB; P80357; -. DR BioCyc; MetaCyc:MONOMER-11524; -. DR BioCyc; PAER208964:G1FZ6-912-MONOMER; -. DR UniPathway; UPA00185; UER00279. DR EvolutionaryTrace; P80357; -. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; P80357; -. DR GO; GO:0008791; F:L-arginine N-succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IBA:GO_Central. DR GO; GO:0006527; P:L-arginine catabolic process; IDA:PseudoCAP. DR Gene3D; 2.40.40.20; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR017651; Arg/Orn_succinylTfrase_asu. DR InterPro; IPR007041; Arg_succinylTrfase_AstA/AruG. DR InterPro; IPR063993; AstA_C. DR NCBIfam; TIGR03245; arg_AOST_alph; 1. DR NCBIfam; TIGR03243; arg_catab_AOST; 1. DR PANTHER; PTHR30420:SF1; ARGININE N-SUCCINYLTRANSFERASE; 1. DR PANTHER; PTHR30420; N-SUCCINYLARGININE DIHYDROLASE; 1. DR Pfam; PF04958; AstA; 1. DR Pfam; PF29831; AstA_C; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PDBsum; 1YLE; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Arginine metabolism; KW Direct protein sequencing; Reference proteome; Transferase. FT CHAIN 1..338 FT /note="Arginine N-succinyltransferase subunit alpha" FT /id="PRO_0000064714" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 12..21 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 33..48 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:1YLE" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 89..99 FT /evidence="ECO:0007829|PDB:1YLE" FT TURN 100..103 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 104..114 FT /evidence="ECO:0007829|PDB:1YLE" FT TURN 116..119 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 120..128 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 136..151 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 175..179 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 220..225 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:1YLE" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 258..263 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 274..280 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 302..307 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:1YLE" FT HELIX 319..325 FT /evidence="ECO:0007829|PDB:1YLE" FT STRAND 332..337 FT /evidence="ECO:0007829|PDB:1YLE" SQ SEQUENCE 338 AA; 36931 MW; 7152BB5EC220F719 CRC64; MLVMRPAQAA DLPQVQRLAA DSPVGVTSLP DDAERLRDKI LASEASFAAE VSYNGEESYF FVLEDSASGE LVGCSAIVAS AGFSEPFYSF RNETFVHASR SLSIHNKIHV LSLCHDLTGN SLLTSFYVQR DLVQSVYAEL NSRGRLLFMA SHPERFADAV VVEIVGYSDE QGESPFWNAV GRNFFDLNYI EAEKLSGLKS RTFLAELMPH YPIYVPLLPD AAQESMGQVH PRAQITFDIL MREGFETDNY IDIFDGGPTL HARTSGIRSI AQSRVVPVKI GEAPKSGRPY LVTNGQLQDF RAVVLDLDWA PGKPVALSVE AAEALGVGEG ASVRLVAV //