ID   A0A2S2DWZ5_9BACT        Unreviewed;       362 AA.
AC   A0A2S2DWZ5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   Name=argE {ECO:0000313|EMBL:AWL09863.1};
GN   ORFNames=HME7025_02014 {ECO:0000313|EMBL:AWL09863.1};
OS   Aquirufa nivalisilvae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Aquirufa.
OX   NCBI_TaxID=2516557 {ECO:0000313|EMBL:AWL09863.1, ECO:0000313|Proteomes:UP000245468};
RN   [1] {ECO:0000313|Proteomes:UP000245468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HME7025 {ECO:0000313|Proteomes:UP000245468};
RA   Kim H., Kang H., Joh K.;
RT   "Pseudarcicella sp. HME7025 Genome sequencing and assembly.";
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}.
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DR   EMBL; CP029346; AWL09863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2DWZ5; -.
DR   KEGG; psez:HME7025_02014; -.
DR   OrthoDB; 9792335at2; -.
DR   Proteomes; UP000245468; Chromosome.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:AWL09863.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245468};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          171..271
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   362 AA;  39774 MW;  4739F82A407D3C20 CRC64;
     MYKESDFLEA KLLITQLIAC PSLSKEEAGT AKIIHDFFEN KGIKSEQFLN NIWAKNAHFD
     PSKPSVLLNS HHDTVKANAS WTFDPWTATE IDGKLIGLGS NDAGASLVCL IQTFCSFYAQ
     ENLPFNLVLA ATAEEEISGK NGIEALLQSP NFPKIDWAIV GEPTDCQMAT AEKGLMVIDA
     VAHGKAGHAA RNEGINAIYV AMKDIQKIEN FQFEKVSPVL GPVKTTVTII NAGKQHNVIP
     DTCEFSIDCR VNECYTLEEV LDILKQELSS DLIPRSIRLQ PSRIDENHVI CLAAKALGLS
     TFGSPTLSDQ SLLTCPSVKI GPGHSGRSHT ADEFIYLDEI KQGIQTYQQL LTQSIIQYQH
     KS
//