ID A0A1I1KXQ4_9BURK Unreviewed; 405 AA.
AC A0A1I1KXQ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00022391, ECO:0000256|HAMAP-Rule:MF_01690};
DE Short=SDAP desuccinylase {ECO:0000256|HAMAP-Rule:MF_01690};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921, ECO:0000256|HAMAP-Rule:MF_01690};
DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000256|ARBA:ARBA00031891, ECO:0000256|HAMAP-Rule:MF_01690};
GN Name=dapE {ECO:0000256|HAMAP-Rule:MF_01690};
GN ORFNames=SAMN05216344_12544 {ECO:0000313|EMBL:SFC62180.1};
OS Polaromonas sp. OV174.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1855300 {ECO:0000313|EMBL:SFC62180.1, ECO:0000313|Proteomes:UP000218980};
RN [1] {ECO:0000313|EMBL:SFC62180.1, ECO:0000313|Proteomes:UP000218980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV174 {ECO:0000313|EMBL:SFC62180.1,
RC ECO:0000313|Proteomes:UP000218980};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_01690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC (2S,6S)-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;
CC Evidence={ECO:0000256|ARBA:ARBA00001246, ECO:0000256|HAMAP-
CC Rule:MF_01690};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01690};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01690};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00005130,
CC ECO:0000256|HAMAP-Rule:MF_01690}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01690}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC {ECO:0000256|ARBA:ARBA00006746, ECO:0000256|HAMAP-Rule:MF_01690}.
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DR EMBL; FOKZ01000025; SFC62180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1KXQ4; -.
DR STRING; 1855300.SAMN05216344_12544; -.
DR OrthoDB; 9809784at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000218980; Unassembled WGS sequence.
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 CDD; cd03891; M20_DapE_proteobac; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
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 NCBIfam; TIGR01246; dapE_proteo; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01690};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_01690};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_01690};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01690};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_01690};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01690}; Reference proteome {ECO:0000313|Proteomes:UP000218980};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01690}.
FT DOMAIN 204..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 97
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
SQ SEQUENCE 405 AA; 43370 MW; E6ACE632AECFB163 CRC64;
MSRTLHLAEQ LISRPSVTPD DAGCQAILAA RLAPLGFSCE TIVSGPEHFR VTNLWAKFEG
FRPAAQSGKA QGAIESIATQ ASGRSRAKTL VFVGHTDVVP TGPLEQWHSH PFTPSHRNGM
LYGRGTADMK TSIAAMVVAV EEFLAAQPQP ELSIAFLITS DEEGPALDGT VVVCEQLKAR
GEVLDYCIVG EPTSVDQLGD MIKNGRRGTL SGKLTIKGVQ GHIAYPHLAK NPIHLFAPAL
AELVATQWDQ GNEFFPATSW QVSNLNGGTG ATNVIPGELV VDFNFRFCTE STPESLQQRL
QAVLSKHQLE YDLKWTLGGL PFLTTPGTLV DAVRGAIQAE TGLNTELSTT GGTSDGRFIA
KICPQVIEFG PINASIHKIN ESVPVASLDP LKNIYKGVLE RLAAA
//
