ID A0A1I7JML8_9BURK Unreviewed; 431 AA.
AC A0A1I7JML8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN05216552_101260 {ECO:0000313|EMBL:SFU86406.1};
OS Pseudoduganella namucuonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFU86406.1, ECO:0000313|Proteomes:UP000199391};
RN [1] {ECO:0000313|Proteomes:UP000199391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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DR EMBL; FPBO01000012; SFU86406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7JML8; -.
DR STRING; 1035707.SAMN05216552_101260; -.
DR Proteomes; UP000199391; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:SFU86406.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:SFU86406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199391};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..431
FT /note="succinyl-diaminopimelate desuccinylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011751589"
FT DOMAIN 214..330
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 431 AA; 45619 MW; A6E4416165EDB65F CRC64;
MKRQLLGALA ACAMQAASAA GLTATEQSIV AAVKANADKG LALLERSVNI NSGTMNHEGV
RAVGKLFRAE FDALGFQTRW IDMPPAVQRA GHLVAERGGK QGKRLLLIGH LDTVFEKDSP
VRLWNRNGNT VRGQGVNDMK GGDVIIIEAL RALHSVGALD NTTITVMFTG DEENAGEPKD
ISRGDMVAAA KRSDIALAFE ATALDAKGQA TGTIGRRASS SWELDVKGKQ GHSSAIFREQ
AGYGAIYEAA RILDGFRQQV VEPDLTFSPG LILGGTGVTH DDAGARGTAH GKTNVIPNTA
MVKGDMRYLS YEQRDRARAK MRAIVAQSLP GTSASISFHD SYPPMSPTAG NLKVLEVYSK
ASEDAGYGPI APLPPGLRGA GDVQFVAPYV DSLDGLGATG NGAHSPDEDL DISSIERATI
RTAILLYRLT R
//
