DAPE_ACIBT
ID DAPE_ACIBT Reviewed; 378 AA.
AC A3M8H2;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=A1S_2810;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-
CC 2,6-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 Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01690};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000255|HAMAP-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000521; ABO13216.2; -; Genomic_DNA.
DR RefSeq; WP_001016573.1; NZ_CP053098.1.
DR PDB; 7T1Q; X-ray; 2.25 A; A/B=1-378.
DR PDBsum; 7T1Q; -.
DR AlphaFoldDB; A3M8H2; -.
DR SMR; A3M8H2; -.
DR KEGG; acb:A1S_2810; -.
DR HOGENOM; CLU_021802_4_0_6; -.
DR UniPathway; UPA00034; UER00021.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cobalt;
KW Diaminopimelate biosynthesis; Hydrolase; Lysine biosynthesis;
KW Metal-binding; Zinc.
FT CHAIN 1..378
FT /note="Succinyl-diaminopimelate desuccinylase"
FT /id="PRO_0000375445"
FT ACT_SITE 70
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:7T1Q"
FT TURN 97..102
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:7T1Q"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:7T1Q"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:7T1Q"
FT HELIX 361..376
FT /evidence="ECO:0007829|PDB:7T1Q"
SQ SEQUENCE 378 AA; 41189 MW; 06FCA9D1E1C19498 CRC64;
MNHSDTLSLS LELLQQPSVT PIDHTCQTIM ADRLAKVGFH IEPMRFGDVD NLWARRGTEG
PVFCFAGHTD VVPTGRLDAW NSDPFAPEIR DGKLYGRGSA DMKTALAAMV VASERFVAKH
PNHKGSIAFL ITSDEEGPAV NGTVKVIETL EKRNEKITWC LVGEPSSTHK LGDIVKNGRR
GSLNAVLKVQ GKQGHVAYPH LARNPIHEAS PALAELCQTV WDNGNEYFPA TSFQISNIHA
GTGATNVIPG ALEVTFNFRY STEVTAEQLK QRVHEILDKH GLQYEIVWNL SGLPFLTPVG
ELVNAAQTAI LNVTGTETEL STSGGTSDGR FIAPTGAQVL ELGVLNATIH QINEHVDVHD
LDPLTDIYEQ ILENLLAQ
