ASTE_SHESA
ID ASTE_SHESA Reviewed; 344 AA.
AC A0KX43;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Shewana3_2132;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000469; ABK48362.1; -; Genomic_DNA.
DR RefSeq; WP_011717095.1; NC_008577.1.
DR AlphaFoldDB; A0KX43; -.
DR SMR; A0KX43; -.
DR STRING; 94122.Shewana3_2132; -.
DR EnsemblBacteria; ABK48362; ABK48362; Shewana3_2132.
DR KEGG; shn:Shewana3_2132; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; KRYLHSD; -.
DR OrthoDB; 632656at2; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000002589; Chromosome.
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; Zinc.
FT CHAIN 1..344
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_1000017330"
FT ACT_SITE 224
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ SEQUENCE 344 AA; 38685 MW; 192B8A4CC60B0D05 CRC64;
MLQALLDSKD FLALTLANPE TLGDEFSFTL GEHTRVEVWN TGVIVFEPAQ AQGKDVILSC
GVHGNETAPI ELCNTLIKQL LQQKIIAKQR TLFLIGNPLA INNGTRIIDE NMNRLFSGEH
SNPPGLVNPE RVRAKKLEAY VDRFFKGAAA GRQRIHYDLH TAMRASKHEK FAIYPYRPGR
AYSAEQIMFL AASGVDTVLF HHEPTTTFSY FSSEQYGADA FTIELGKVYP MGQNDMTRFI
AAQEMFMRLI TDKPLALEPF SADKVNLYQV CRVINKHFDD FEFTFAADVE NFRSFPKGFV
LAREGGQEIK VEQEFEAIVF PNAKVPIGNR TVICLIPSVA PDVR