ID A0A1R4GGU8_9MICC Unreviewed; 401 AA.
AC A0A1R4GGU8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=FM101_10355 {ECO:0000313|EMBL:SJM67295.1};
OS Arthrobacter rhombi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=71253 {ECO:0000313|EMBL:SJM67295.1, ECO:0000313|Proteomes:UP000195913};
RN [1] {ECO:0000313|EMBL:SJM67295.1, ECO:0000313|Proteomes:UP000195913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Ar 00.02 {ECO:0000313|EMBL:SJM67295.1,
RC ECO:0000313|Proteomes:UP000195913};
RA Peterson S.W.;
RL Submitted (FEB-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}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; FUHW01000037; SJM67295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4GGU8; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000195913; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd08659; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
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; TIGR01910; DapE-ArgE; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SJM67295.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000195913};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 187..288
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 401 AA; 41916 MW; D24CE0748FD69850 CRC64;
MAETATGATA WQVDTSVLTA LTIELVNAGG VNPGGTEQAT VDVLVAEARR RGLQVTTREV
EPGRPNVFIT LPGGQGPGLL FLGHSDVVPV GDGWDRDPFD AYVADGRLFG RGATDMKGGL
AAILTSMTML HDAGTQLSGP VTLACLVDEE ETGAGIRALV ADGLDHPYLG CVVAEPTDLE
TVIACRGDSY LEVEVTGQAA HSGRPSDGRN AIDAAVRICN LVTADQERLR AENDPLLGYA
TWNTGMVSGG RGTSMVAPEA HLWFDRRLMP GEDTTSIRED LLSRIDAAGI TGDGISVQLR
TTMEMPGFRT EPDHPLVTAA LAALAEAGVQ TRVSGWTASC DGGFISRDLG IPSIVLGPGE
LNEEAHQPNE SVRVSEVIAA TRAYGMLIST LLNPDYGASG A
//
