ID   ASTE_ECOLI              Reviewed;         322 AA.
AC   P76215; Q2MB41;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Succinylglutamate desuccinylase;
DE            EC=3.5.1.96 {ECO:0000269|PubMed:9696779};
GN   Name=astE; Synonyms=ydjS; OrderedLocusNames=b1744, JW1733;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-322.
RC   STRAIN=K12;
RX   PubMed=9068658; DOI=10.1128/jb.179.6.2073-2076.1997;
RA   Hagenmaier S., Stierhof Y.-D., Henning U.;
RT   "A new periplasmic protein of Escherichia coli which is synthesized in
RT   spheroplasts but not in intact cells.";
RL   J. Bacteriol. 179:2073-2076(1997).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9696779; DOI=10.1128/jb.180.16.4278-4286.1998;
RA   Schneider B.L., Kiupakis A.K., Reitzer L.J.;
RT   "Arginine catabolism and the arginine succinyltransferase pathway in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:4278-4286(1998).
RN   [5]
RP   PREDICTION OF ZINC-BINDING RESIDUES AND ACTIVE SITE.
RX   PubMed=10493853; DOI=10.1006/jmbi.1999.3059;
RA   Makarova K.S., Grishin N.V.;
RT   "The Zn-peptidase superfamily: functional convergence after evolutionary
RT   divergence.";
RL   J. Mol. Biol. 292:11-17(1999).
RN   [6]
RP   INDUCTION.
RX   PubMed=12003934; DOI=10.1128/jb.184.11.2940-2950.2002;
RA   Kiupakis A.K., Reitzer L.;
RT   "ArgR-independent induction and ArgR-dependent superinduction of the
RT   astCADBE operon in Escherichia coli.";
RL   J. Bacteriol. 184:2940-2950(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RG   Northeast structural genomics consortium (NESG);
RT   "Crystal structure of succinylglutamate desuccinylase from Escherichia
RT   coli, Northeast structural genomics target Et72.";
RL   Submitted (MAY-2005) to the PDB data bank.
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate. {ECO:0000269|PubMed:9696779}.
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:0000269|PubMed:9696779};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15170;
CC         Evidence={ECO:0000305|PubMed:9696779};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC       {ECO:0000305|PubMed:9696779}.
CC   -!- INTERACTION:
CC       P76215; P0ACS9: acrR; NbExp=3; IntAct=EBI-1121806, EBI-1117360;
CC   -!- INDUCTION: By nitrogen starvation, and arginine. Induced at stationary
CC       phase by sigma S. {ECO:0000269|PubMed:12003934}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily. {ECO:0000305}.
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DR   EMBL; U00096; AAC74814.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76515.1; -; Genomic_DNA.
DR   PIR; H64933; H64933.
DR   RefSeq; NP_416258.1; NC_000913.3.
DR   RefSeq; WP_000368506.1; NZ_SSZK01000001.1.
DR   PDB; 1YW6; X-ray; 3.10 A; A/B=1-322.
DR   PDBsum; 1YW6; -.
DR   AlphaFoldDB; P76215; -.
DR   SMR; P76215; -.
DR   BioGRID; 4262239; 18.
DR   BioGRID; 850616; 4.
DR   IntAct; P76215; 10.
DR   STRING; 511145.b1744; -.
DR   jPOST; P76215; -.
DR   PaxDb; 511145-b1744; -.
DR   EnsemblBacteria; AAC74814; AAC74814; b1744.
DR   GeneID; 946256; -.
DR   KEGG; ecj:JW1733; -.
DR   KEGG; eco:b1744; -.
DR   PATRIC; fig|1411691.4.peg.512; -.
DR   EchoBASE; EB3751; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   InParanoid; P76215; -.
DR   OMA; CAVHGNE; -.
DR   OrthoDB; 5290473at2; -.
DR   PhylomeDB; P76215; -.
DR   BioCyc; EcoCyc:SUCCGLUDESUCC-MONOMER; -.
DR   BioCyc; MetaCyc:SUCCGLUDESUCC-MONOMER; -.
DR   BRENDA; 3.5.1.96; 2026.
DR   UniPathway; UPA00185; UER00283.
DR   EvolutionaryTrace; P76215; -.
DR   PRO; PR:P76215; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
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; IDA:EcoCyc.
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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00767; Arg_catab_AstE; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   NCBIfam; TIGR03242; arg_catab_astE; 1.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF017020; AstE; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Arginine metabolism; Hydrolase; Metal-binding;
KW   Reference proteome; Stress response; Zinc.
FT   CHAIN           1..322
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_0000174639"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000255"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   HELIX           1..10
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          18..30
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           58..71
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           117..134
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          153..161
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           194..201
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          205..210
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   HELIX           225..236
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          249..255
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          296..302
FT                   /evidence="ECO:0007829|PDB:1YW6"
FT   STRAND          316..321
FT                   /evidence="ECO:0007829|PDB:1YW6"
SQ   SEQUENCE   322 AA;  35800 MW;  6602BAD75AB0A893 CRC64;
     MDNFLALTLT GKKPVITERE INGVRWRWLG DGVLELTPLT PPQGALVISA GIHGNETAPV
     EMLDALLGAI SHGEIPLRWR LLVILGNPPA LKQGKRYCHS DMNRMFGGRW QLFAESGETC
     RARELEQCLE DFYDQGKESV RWHLDLHTAI RGSLHPQFGV LPQRDIPWDE KFLTWLGAAG
     LEALVFHQEP GGTFTHFSAR HFGALACTLE LGKALPFGQN DLRQFAVTAS AIAALLSGES
     VGIVRTPPLR YRVVSQITRH SPSFEMHMAS DTLNFMPFEK GTLLAQDGEE RFTVTHDVEY
     VLFPNPLVAL GLRAGLMLEK IS
//