ID A0A1H8KNW1_9RHOB Unreviewed; 382 AA.
AC A0A1H8KNW1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN04488103_109153 {ECO:0000313|EMBL:SEN94564.1};
OS Gemmobacter aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=933059 {ECO:0000313|EMBL:SEN94564.1, ECO:0000313|Proteomes:UP000198761};
RN [1] {ECO:0000313|EMBL:SEN94564.1, ECO:0000313|Proteomes:UP000198761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3857 {ECO:0000313|EMBL:SEN94564.1,
RC ECO:0000313|Proteomes:UP000198761};
RA de Groot N.N.;
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}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691}.
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DR EMBL; FOCE01000009; SEN94564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8KNW1; -.
DR STRING; 933059.SAMN04488103_109153; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000198761; 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; PS00758; ARGE_DAPE_CPG2_1; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198761};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 167..276
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 382 AA; 40117 MW; CB2D432A8A7E0BF2 CRC64;
MRGIFETLMA FDTVSAKPNM ALMAYVRDLL ADAGITAHLI PDATGQKANL FATTGPQGVG
GVMLSGHTDV VPVEGQAWTK PPFALTEADG RFYGRGAADM KGFCALAIDA MLKASTRDLK
VPLHLALSYD EEIGCMGVRS LVDLLALAPV KPRFCIVGEP TGMQVATGHK GKVALRATCT
GREGHSALAP LALNALHLAA DFLNAVRALQ ARVAESGHRD GDYDVPYSTI HVGKMAGGVQ
VNIVPNTATL DFEIRSLAED DPETLIADLR AAAETIVAPL RATFPEAEIR VERLWDYPGL
GTPSDAAVVN FVKGLTGANG TIKVAFGTEG GLFAQHLGIP TVICGPGSMA QGHKPDEFVT
VEQMARGAAM LDALLARCEA GF
//