ID A0A1R0UDU0_9MYCO Unreviewed; 358 AA.
AC A0A1R0UDU0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=A5736_17125 {ECO:0000313|EMBL:OMC17084.1};
OS Mycobacterium sp. SP-6446.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834162 {ECO:0000313|EMBL:OMC17084.1, ECO:0000313|Proteomes:UP000187139};
RN [1] {ECO:0000313|Proteomes:UP000187139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-6446 {ECO:0000313|Proteomes:UP000187139};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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}.
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:OMC17084.1}.
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DR EMBL; MBEM01000102; OMC17084.1; -; Genomic_DNA.
DR RefSeq; WP_076245599.1; NZ_MBEM01000102.1.
DR AlphaFoldDB; A0A1R0UDU0; -.
DR Proteomes; UP000187139; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
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 InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR NCBIfam; TIGR01900; dapE-gram_pos; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 170..268
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 358 AA; 37783 MW; 7D6614DE594B95B5 CRC64;
MLDLHGDPIE LTAALVDIPS ESRDEARIAD EVEAALRAQT SGFEIVRNGN AVLARTQRNR
PSRVLLAGHL DTVPVADNVP SRRSTEPEGD VLHGCGTADM KSGDAVFLHL AATIAEPVHD
LTLVFYDCEE IDAAANGLGR IERELPDWLS ADVAILGEPT AGYIEAGCQG TLRVVISATG
TRAHSARSWL GDNAIHKLGA VLDRLARYSA RTVDIDGCTY REGLSAVRVD GGVAGNVIPD
AAAVTVNYRF APDRSLDAAL QHVHDVFDGL DVRIEQTDAA AGALPGLSQP AAKALVEAAG
GQVRAKYGWT DVSRFAARGI PAVNFGPGDP NLAHRRDERV QVAAITAAAA MLRPYLGG
//
