ASTA_PSEAE
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 03-AUG-2022, entry version 132.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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 / 1C /
RC 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 / 1C /
RC 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=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;
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}.
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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; NZ_QZGE01000007.1.
DR PDB; 1YLE; X-ray; 1.70 A; A=1-338.
DR PDBsum; 1YLE; -.
DR AlphaFoldDB; P80357; -.
DR SMR; P80357; -.
DR STRING; 287.DR97_1047; -.
DR DrugBank; DB01942; Formic acid.
DR PaxDb; P80357; -.
DR PRIDE; P80357; -.
DR DNASU; 879437; -.
DR EnsemblBacteria; AAG04285; AAG04285; PA0896.
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 OMA; ETDHYID; -.
DR PhylomeDB; P80357; -.
DR BioCyc; MetaCyc:MON-11524; -.
DR BioCyc; PAER208964:G1FZ6-912-MON; -.
DR UniPathway; UPA00185; UER00279.
DR EvolutionaryTrace; P80357; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008791; F:arginine N-succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR017651; Arg/Orn_succinylTfrase_asu.
DR InterPro; IPR007041; Arg_succinylTrfase_AstA/AruG.
DR Pfam; PF04958; AstA; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03245; arg_AOST_alph; 1.
DR TIGRFAMs; TIGR03243; arg_catab_AOST; 1.
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
