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Database: UniProt
Entry: A9I633_BORPD
LinkDB: A9I633_BORPD
Original site: A9I633_BORPD 
ID   A9I633_BORPD            Unreviewed;       326 AA.
AC   A9I633;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Succinylglutamate desuccinylase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Bpet3916 {ECO:0000313|EMBL:CAP44262.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44262.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP44262.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; AM902716; CAP44262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I633; -.
DR   STRING; 94624.Bpet3916; -.
DR   KEGG; bpt:Bpet3916; -.
DR   eggNOG; COG3608; Bacteria.
DR   OMA; TSMDFRF; -.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAP44262.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35283 MW;  51F476AFFB48ED6A CRC64;
     MQFQLSAPDL SAERAGNTGT PGVWHFDSGT PGRALMVTAL VHGNELCGAW ALKELLASGL
     RPRRGSLTLA FCNLEAFDRF DSARHDASRF VDEDLNRVWS AQRLDDPVSC ERRRGAALRP
     WVERADWLLD LHSMHEPGAP LLLTGVLPRN IALARRLGAP RHVIVDAGHQ DGVRMRDYGR
     FGDPGQADAC ALLIECGFHG DPAARLAARD LVARMLVESA VIDATDMPDG WLLPDTPPDQ
     ACGALHGAGP QRVLQVTDAV VAPSMDLRFA QPWQGLETLA EAGSLIGWAD GAPVVTPYDN
     CTLIMPSLRQ LKPGVTVVRL AREYAG
//
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