ID W6U2J7_9SPHI Unreviewed; 355 AA.
AC W6U2J7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=N824_11910 {ECO:0000313|EMBL:ETZ19441.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19441.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ19441.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ19441.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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:ETZ19441.1}.
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DR EMBL; AWRU01000034; ETZ19441.1; -; Genomic_DNA.
DR RefSeq; WP_048908225.1; NZ_AWRU01000034.1.
DR AlphaFoldDB; W6U2J7; -.
DR STRING; 509635.N824_11910; -.
DR PATRIC; fig|509635.5.peg.5358; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000019145; 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 CDD; cd05651; M20_ArgE_DapE-like; 1.
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 167..265
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 355 AA; 39353 MW; 56CCCF18BE2F0643 CRC64;
MIEQLQKDSL ELLKELIGIQ SFSKEEDKTA DAIEQFLQQR DIKTYRKLNN IWAYNKHFDT
NKPTVLLNSH HDTVKPNSGY TRDPYDAAVE DGKLYGLGSN DAGGCLVSLI ATFLYFYNQE
ELSYNICLAT TAEEEISGNN GLECVLPDLG ELEFAIVGEP TQMNLAIAER GLLVLDCIST
GKAGHAAREE GDNAIYKALK DIEWFRNYRF SKISEVFGPL KMSVTIINAG SQHNVVPATC
TFTVDVRVTD AYTNEEVLKI IRTNVDCEVT PRSIRLKPSS IDKEHPLVQS GIALGRTTYG
SPTTSDQALL SIPSVKVGPG DSARSHMADE YVYVNEIAEG IELYIDMLKP VIKGK
//
