ID A0A1G4XAG1_9ACTN Unreviewed; 373 AA.
AC A0A1G4XAG1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN03159343_0312 {ECO:0000313|EMBL:SCX38137.1};
OS Klenkia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=1960309 {ECO:0000313|EMBL:SCX38137.1, ECO:0000313|Proteomes:UP000198981};
RN [1] {ECO:0000313|Proteomes:UP000198981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45722 {ECO:0000313|Proteomes:UP000198981};
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; FMUH01000001; SCX38137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4XAG1; -.
DR STRING; 1960309.SAMN03159343_0312; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000198981; 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; PS00759; ARGE_DAPE_CPG2_2; 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 177..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 373 AA; 39016 MW; B949D08E06DE9AF5 CRC64;
MTAPGLDLSA DVLALTRALV DLPSVSGTEG PLADLVETAL RGLGGLEVVR IGNNVLARTD
LGRDTRVVLA GHLDTVPVAD NVPSRRETVD GEDRLYGCGT SDMKAGDALM LRVAGMFGTP
GAAPARDLTF VFYDNEEVEA VKNGLGQVAR ELRGWLYGDL AILLEPTDGD VEGGCQGTMR
VVLTVPGKRA HSARSWLGAN AIHGASSILA VLGAYEAREV EIDGLHFHEG LNAVRIEGGV
AGNVVPDECR VTVNFRFAPD RDEDDAEAHV REVFADALAA GVTLEVTDMS GGALPGLAEP
AAAEFVAAVG RPARAKLGWT DVARFAAFGI PAVNYGPGDP NQAHQRGEHV RVDRLQPAED
ALIAYLTSTG SAA
//
