ASTE_PSEAE
ID ASTE_PSEAE Reviewed; 332 AA.
AC O50177;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Succinylglutamate desuccinylase {ECO:0000255|HAMAP-Rule:MF_00767};
DE EC=3.5.1.96 {ECO:0000255|HAMAP-Rule:MF_00767};
GN Name=astE {ECO:0000255|HAMAP-Rule:MF_00767}; Synonyms=aruE;
GN OrderedLocusNames=PA0901;
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).
CC -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-L-glutamate = L-glutamate + succinate;
CC Xref=Rhea:RHEA:15169, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58763; EC=3.5.1.96;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00767};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
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; AAC46014.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04290.1; -; Genomic_DNA.
DR PIR; F83533; F83533.
DR RefSeq; NP_249592.1; NC_002516.2.
DR RefSeq; WP_003112605.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; O50177; -.
DR SMR; O50177; -.
DR STRING; 287.DR97_1042; -.
DR PaxDb; O50177; -.
DR PRIDE; O50177; -.
DR EnsemblBacteria; AAG04290; AAG04290; PA0901.
DR GeneID; 878165; -.
DR KEGG; pae:PA0901; -.
DR PATRIC; fig|208964.12.peg.936; -.
DR PseudoCAP; PA0901; -.
DR HOGENOM; CLU_071608_0_0_6; -.
DR InParanoid; O50177; -.
DR OMA; KRYLHSD; -.
DR PhylomeDB; O50177; -.
DR BioCyc; PAER208964:G1FZ6-917-MON; -.
DR BRENDA; 3.5.1.96; 5087.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
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 CDD; cd03855; M14_ASTE; 1.
DR HAMAP; MF_00767; Arg_catab_AstE; 1.
DR InterPro; IPR007036; Aste_AspA.
DR InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF017020; AstE; 1.
DR TIGRFAMs; TIGR03242; arg_catab_astE; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..332
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174643"
FT ACT_SITE 215
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ SEQUENCE 332 AA; 36909 MW; EE8F131836747F59 CRC64;
MLALGKLLDL TLAGREPTEK IQLTADGTRL HWLAEGALEV TPIGARDNGV DLLLSAGIHG
NETAPIELLE RLIRKVAAGT LKPAARVLFL FGNPEAIRRG ERYVEQDMNR LFNGRHEEGS
GNEAFRAAEL ERLAQVFFSK TERVHLHYDL HTAIRGSKIE QFALYPWAEG RQHSRSELAR
LRDAGIEAVL LQNKPGITFS AYTYGQLGAE AFTLELGKAR PFGENQEVNL ERLERSLELL
IDGSEEQPDG SRLDGLKLFS VSREVIKHSD HFRLHLDDDV ANFTELSPGY LLAEDIGGTR
WVVDEVGARI IFPNPRVKNG LRAGILVVPA KL
