ASTE_YERPE
ID ASTE_YERPE Reviewed; 330 AA.
AC Q9ZC70; Q0WFI3; Q8D0D9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
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};
GN OrderedLocusNames=YPO1966, y2345, YP_1711;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6/69;
RA Buchrieser C., Rusniok C., Couve E., Frangeul L., Billault A., Kunst F.,
RA Carniel E., Glaser P.;
RT "DNA sequence of the 102 kbases unstable region of Yersinia pestis.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM85903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS61940.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL031866; CAA21337.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20604.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85903.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61940.1; ALT_INIT; Genomic_DNA.
DR PIR; AI0239; AI0239.
DR PIR; T46994; T46994.
DR RefSeq; WP_002212028.1; NZ_WUCM01000003.1.
DR RefSeq; YP_002346955.1; NC_003143.1.
DR AlphaFoldDB; Q9ZC70; -.
DR SMR; Q9ZC70; -.
DR STRING; 214092.YPO1966; -.
DR PaxDb; Q9ZC70; -.
DR DNASU; 1147292; -.
DR EnsemblBacteria; AAM85903; AAM85903; y2345.
DR EnsemblBacteria; AAS61940; AAS61940; YP_1711.
DR GeneID; 66841606; -.
DR KEGG; ype:YPO1966; -.
DR KEGG; ypk:y2345; -.
DR KEGG; ypm:YP_1711; -.
DR PATRIC; fig|214092.21.peg.2343; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; KRYLHSD; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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: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..330
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174654"
FT ACT_SITE 210
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ SEQUENCE 330 AA; 37268 MW; 6938845D7219BEDA CRC64;
MLDFLAITLS GKPPQVIQGE TVNLKWQWLG EGILTLVPHR SYTQSVVISA GIHGNETAPI
EILNQLVTDL LAGQLPLSVR LLVLLGNPPA IRKGKRYLSN DINRMFGGRY QHYTPSDETR
RASTLEQRVM AFFQASHTSE RLHYDLHTAI RGSYHPRFGL LPYQQTPYSA AMFRWLRDIE
LDALVMHTSA GGTFAHFSSE RCQAASCTLE LGKALPFGEN QLSQFSAITQ GLRSLVSDSA
LPARKTENMK YYRVVKSLLR QHPDFKLRVA EDTVNFTRFA QGTLLTEQPN DNYRVEHPYE
WILFPNPHVA LGLRAGMMLV KMCESELPIT
