ID A0A2V4BQY0_9FLAO Unreviewed; 356 AA.
AC A0A2V4BQY0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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=DMB65_07710 {ECO:0000313|EMBL:PXY41448.1};
OS Flavobacterium cheongpyeongense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2212651 {ECO:0000313|EMBL:PXY41448.1, ECO:0000313|Proteomes:UP000247903};
RN [1] {ECO:0000313|EMBL:PXY41448.1, ECO:0000313|Proteomes:UP000247903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC34759 {ECO:0000313|EMBL:PXY41448.1,
RC ECO:0000313|Proteomes:UP000247903};
RA Joung Y., Cho J.;
RT "Flavobacterium sp. strain IMCC34759, incomplete genome.";
RL Submitted (MAY-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:PXY41448.1}.
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DR EMBL; QJHK01000005; PXY41448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4BQY0; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000247903; 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 Reference proteome {ECO:0000313|Proteomes:UP000247903};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 169..272
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 356 AA; 39405 MW; 4BC974D029B61BA6 CRC64;
MKNIETLTRE AIELLRNLIE TPSFSSEEDQ TALLIENWFT QNGIPFKREN NNVWAFNKYF
DEKKPTLLLN SHHDTVRPNQ AYTNDPFKAI EKDGKLFGLG SNDAGGCLVS LLATFVHFYE
NQNLSHNLVI VASAEEESSG KNGLNSVLKH LPELDCAIVG EPTLMQLAVA EKGLLVLDVK
VKGTASHAAH QNDDNALYKS IPVMEWFKNY KFDKVSEVLG PVKMTVTQIN AGKQHNVVPS
ECDLVVDIRV NDCYTNSEIL EVVTASVNAE VKPRSMHLNA SSIPIAHGLV QAGIALGRMT
YGSPTLSDQS VLSCQSLKLG PGETLRSHSA DEFIFVNEIE EGVDLYIKIL TDFFKL
//
