(data stored in ACNUC7421 zone)

SWISSPROT: DAPE_RHOPS

ID   DAPE_RHOPS              Reviewed;         388 AA.
AC   Q13F22;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=RPD_0077;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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; CP000283; ABE37317.1; -; Genomic_DNA.
DR   RefSeq; WP_011500510.1; NC_007958.1.
DR   SMR; Q13F22; -.
DR   STRING; 316057.RPD_0077; -.
DR   MEROPS; M20.010; -.
DR   PRIDE; Q13F22; -.
DR   EnsemblBacteria; ABE37317; ABE37317; RPD_0077.
DR   KEGG; rpd:RPD_0077; -.
DR   eggNOG; ENOG4105C9Y; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243770; -.
DR   KO; K01439; -.
DR   OMA; LNSHHDT; -.
DR   OrthoDB; 275025at2; -.
DR   BioCyc; RPAL316057:RPD_RS00385-MONOMER; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q13F22.
DR   SWISS-2DPAGE; Q13F22.
KW   Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Metal-binding; Zinc.
FT   CHAIN           1..388
FT                   /note="Succinyl-diaminopimelate desuccinylase"
FT                   /id="PRO_0000375692"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   ACT_SITE        142
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           74
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           107
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           107
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           143
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           171
FT                   /note="Cobalt or zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   METAL           360
FT                   /note="Cobalt or zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
SQ   SEQUENCE   388 AA;  40959 MW;  AD5A996A74DB7DFC CRC64;
     MTSSRDALSI AQALLRCPSV TPADAGALGV LETLLKDAGF TAHRVTFSEP GAADIDNLYA
     RIGDGAPHLC FAGHTDVVPP GDADAWSHGA FSGDVEGGLL YGRGAVDMKG GIACAVAAVL
     DHLAAHGGRP KGSISFLITG DEEDVAVNGT VKLLQWAADR GETFDHCIVG EPSNVEAIGD
     TIKIGRRGSQ SGMLIVDGLQ GHVAYPHRAS NPIPDIAALI TALNDEPLDQ GSAQFQPSNL
     EFTSVDVGNP ATNVIPAQAR AKFNIRFNDH HTQDSLKALI EQRLAAACGN RIRARIEWLP
     SNADVFVTKP GNFTDLVTAS IADVTGRTPD LNTGGGTSDA RFIAKYCPVV EFGLVGQTMH
     QIDERTPVAD LDQLTAIYRG VLERYFKS
//

If you have problems or comments...

PBIL Back to PBIL home page