(data stored in SCRATCH zone)

SWISSPROT: DAPE_SALAR

ID   DAPE_SALAR              Reviewed;         375 AA.
AC   A9MHQ8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690};
DE            Short=SDAP desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690};
DE            EC=3.5.1.18 {ECO:0000255|HAMAP-Rule:MF_01690};
DE   AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01690};
GN   Name=dapE {ECO:0000255|HAMAP-Rule:MF_01690}; OrderedLocusNames=SARI_00399;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic
CC       acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP),
CC       an intermediate involved in the bacterial biosynthesis of lysine and
CC       meso-diaminopimelic acid, an essential component of bacterial cell
CC       walls. {ECO:0000255|HAMAP-Rule:MF_01690}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-LL-2,6-diaminopimelate = LL-2,6-
CC         diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58087; EC=3.5.1.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01690};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01690};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01690};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01690};
CC       Note=Binds 1 Co(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01690};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 3/3. {ECO:0000255|HAMAP-Rule:MF_01690}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01690}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01690}.
DR   EMBL; CP000880; ABX20336.1; -; Genomic_DNA.
DR   RefSeq; WP_001277825.1; NC_010067.1.
DR   SMR; A9MHQ8; -.
DR   EnsemblBacteria; ABX20336; ABX20336; SARI_00399.
DR   KEGG; ses:SARI_00399; -.
DR   eggNOG; ENOG4105C9Y; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243770; -.
DR   KO; K01439; -.
DR   OMA; LNSHHDT; -.
DR   OrthoDB; 275025at2; -.
DR   BioCyc; SENT882884:G1GAH-391-MONOMER; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01690; DapE; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR005941; DapE_proteobac.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01246; dapE_proteo; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A9MHQ8.
DR   SWISS-2DPAGE; A9MHQ8.
KW   Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..375
FT                   /note="Succinyl-diaminopimelate desuccinylase"
FT                   /id="PRO_0000375712"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           66
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           99
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           99
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           134
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           162
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           348
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
SQ   SEQUENCE   375 AA;  41578 MW;  ED6165EDEEB262A0 CRC64;
     MSCPVIELTQ QLIRRPSLSP DDAGCQALMI ERLRKIGFTI EHMDFGDTQN FWAWRGRGET
     LAFAGHTDVV PAGDVDRWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPH
     HRGRLAFLIT SDEEASAKNG TVKVVEALMA RNERLDYCLV GEPSSTEIVG DVVKNGRRGS
     LTCNLTIHGV QGHVAYPHLA DNPVHRAAPF LNELVAIEWD RGNDFFPATS MQVANIQAGT
     GSNNVIPGEL FVQFNFRFST ELTDEMIKER VHALLEKHQL RYTVDWWLSG QPFLTARGKL
     VDAVVNAIEH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVNAADLQ
     LLARMYQRIM EQLVA
//

If you have problems or comments...

PBIL Back to PBIL home page