ID A0A418NWQ6_9SPHN Unreviewed; 439 AA.
AC A0A418NWQ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=D2V07_01880 {ECO:0000313|EMBL:RIV89032.1};
OS Aurantiacibacter zhengii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV89032.1, ECO:0000313|Proteomes:UP000286576};
RN [1] {ECO:0000313|EMBL:RIV89032.1, ECO:0000313|Proteomes:UP000286576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V18 {ECO:0000313|EMBL:RIV89032.1,
RC ECO:0000313|Proteomes:UP000286576};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-2018) 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:RIV89032.1}.
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DR EMBL; QXFL01000001; RIV89032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418NWQ6; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000286576; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286576};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..439
FT /note="succinyl-diaminopimelate desuccinylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019536911"
FT DOMAIN 216..333
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 439 AA; 46029 MW; 1E0A8CAF928FDAF9 CRC64;
MSSRIASGLL VGSAIALSAP AHAQITPAEQ VMIQSVEASF ENDVALLEAI TNVNSGTYNH
DGVREVGQML MPEFEALGFD VEWIDQSHVD RAGHLFARRE GDPDSTRILM IGHIDTVFEP
DSPFQQFVRD GDTATGPGVV DDKGGIVVIL SSLRAMQAAG TLDGANIVVA LTGDEEDAGD
PIAQSRQHLI EAGQWADVAL GFEGLSVVDG RDMGVVARRS SNSWTLTTTG RTGHSSRVFS
EGSGYGAIYE MARILDGFRT QLPEENLTYN VGFMAGGTPA ALGDDNLSAA GSGKTNIIPS
DAVARGDLRT LTQEQTDRAV AAMQAIVDAN LPGTDATIEF EFSYPPMSPT EGSSALLARL
NAINADMGLG EMGIYPPALR GAADISFVAP YADGLAGMGP DGSGSHAVGE SADLRSFTRQ
AQRAAILMSR LAAETPARD
//
