ID A0A3S2WNK7_9RHOB Unreviewed; 387 AA.
AC A0A3S2WNK7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN Name=argE {ECO:0000313|EMBL:RVT84024.1};
GN ORFNames=DXV76_09995 {ECO:0000313|EMBL:RVT84024.1};
OS Rhodobacteraceae bacterium CCMM004.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT84024.1, ECO:0000313|Proteomes:UP000287438};
RN [1] {ECO:0000313|EMBL:RVT84024.1, ECO:0000313|Proteomes:UP000287438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM004 {ECO:0000313|EMBL:RVT84024.1,
RC ECO:0000313|Proteomes:UP000287438};
RA Zhang Z.;
RT "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT culture.";
RL Submitted (JAN-2019) 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 -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691}.
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:RVT84024.1}.
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DR EMBL; RZWH01000003; RVT84024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2WNK7; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000287438; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03894; M20_ArgE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010169; AcOrn-deacetyl.
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 NCBIfam; TIGR01892; AcOrn-deacetyl; 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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RVT84024.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000287438};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 173..284
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 387 AA; 41883 MW; 524B19188B8BB79F CRC64;
MPRRLTARDI MDKLVSFPTV SRDSNLDLID WVEDYLDGHG VRATRVWDAG RDKASLYANV
GPQVEGGIVL SGHTDVVPVD GQDWTSDPFT VTERNGRLYG RGTCDMKGFD ALALAAVPLA
LERGVKRPLQ IALSYDEEVG CTGAPPMIDE MVAHLPRAAA AIIGEPSTMQ VVTGHKGGAG
YRVRMRGFEV HSSIMHQGVS AVMEAARLID WANRMNAENR AAAPGPLAAD FDPPWTTLHV
GMVQGGTAHN ITAKDCEFLL SWRVVPGESS EDWGARFLAE VARIEAEMKA VRPEAGIDLE
KYFDVPALAQ EDAGEAERLT RMLTGDNGTH AVSYATEAGQ FQARGYSAVV CGPGDIAQAH
QPDEYIEAAQ LAAGEAFMER LVDHLCR
//
