ID A0A212UDV5_9BACT Unreviewed; 356 AA.
AC A0A212UDV5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN06265337_3380 {ECO:0000313|EMBL:SNC76427.1};
OS Hymenobacter gelipurpurascens.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=89968 {ECO:0000313|EMBL:SNC76427.1, ECO:0000313|Proteomes:UP000198131};
RN [1] {ECO:0000313|EMBL:SNC76427.1, ECO:0000313|Proteomes:UP000198131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11116 {ECO:0000313|EMBL:SNC76427.1,
RC ECO:0000313|Proteomes:UP000198131};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FYEW01000002; SNC76427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212UDV5; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000198131; 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 170..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 356 AA; 39320 MW; 132BA54397A2CFA6 CRC64;
MPELIEQLTE DAIELLQELI QTPSLSREED QTAELIFRFL TFHGTHPRRD KNNVWAVSKH
FDPSKPTILL NSHHDTVKAG NTWTYDPLGA TVEDDKLIGL GSNDAGASAV SLLATFLYFH
ERPDLAYNLV CAITAEEEIS GVNGIRSVLP QLGHIDLGIV GEPTQMDLAV AEKGLVVLDC
VAHGRTGHAA REEGENALYK AVADIRWFEQ FRFPEVSPLL GPVKMTVTQI QAGSQHNVVP
DRCTFVVDVR TNECYSNPDV VELVRRHVTS DVTPRSTHLN SSRIELDHPL VQRGIGLGRR
TFGSVTLSDQ SMMLFTTVKI GPGDSARSHT PDEYILLSEI RAGVRGYIEL LDGLVL
//
