ID A0A010S1V6_PSEFL Unreviewed; 383 AA.
AC A0A010S1V6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=HK44_028050 {ECO:0000313|EMBL:EXF94784.1};
OS Pseudomonas fluorescens HK44.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF94784.1, ECO:0000313|Proteomes:UP000022611};
RN [1] {ECO:0000313|EMBL:EXF94784.1, ECO:0000313|Proteomes:UP000022611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK44 {ECO:0000313|EMBL:EXF94784.1,
RC ECO:0000313|Proteomes:UP000022611};
RX PubMed=21742869; DOI=10.1128/JB.05530-11;
RA Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA Karpinets T.V., Brown S.D., Sayler G.S.;
RT "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT HK44.";
RL J. Bacteriol. 193:5009-5010(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF94784.1}.
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DR EMBL; AFOY02000009; EXF94784.1; -; Genomic_DNA.
DR RefSeq; WP_019692074.1; NZ_AFOY02000009.1.
DR AlphaFoldDB; A0A010S1V6; -.
DR PATRIC; fig|1042209.11.peg.2185; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_4_0_6; -.
DR OrthoDB; 9809784at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000022611; 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; 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 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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 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:UP000022611};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01690}.
FT DOMAIN 183..290
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 75
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01690"
SQ SEQUENCE 383 AA; 41172 MW; C52BE1DA3A70D53C CRC64;
MTAHADLSPT LQLAIDLIRR PSVTPVDADC QKQMMQRLGD AGFALEPMRI EDVDNFWATH
GKHEGPVLCF AGHTDVVPTG PVQAWQIDPF DAVIDEHGML CGRGAADMKG SLASMTVAAE
RFVADYPDHK GKVAFLITSD EEGPAHHGTK AVVERLAARK ERLDWCIVGE PSSTTLVGDV
VKNGRRGSLG AKLTVRGVQG HVAYPHLAKN PIHLTAPALA ELAAEHWDHG NDFFPPTSFQ
ISNVNSGTGA TNVIPGDLVA VFNFRFSTES TVEGLQQRVA DILDKHGLDW HIDWALSGLP
FLTEPGALLD AVSASIKTIT GRETKASTSG GTSDGRFIAT LGTQVVELGP VNATIHQVNE
RVLASDLDLL TEIYYQTLIK LLA
//
