ID A0QV93_MYCS2 Unreviewed; 390 AA.
AC A0QV93;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN OrderedLocusNames=MSMEG_2491 {ECO:0000313|EMBL:ABK75619.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75619.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK75619.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000480; ABK75619.1; -; Genomic_DNA.
DR RefSeq; WP_011728380.1; NZ_SIJM01000012.1.
DR RefSeq; YP_886831.1; NC_008596.1.
DR AlphaFoldDB; A0QV93; -.
DR STRING; 246196.MSMEG_2491; -.
DR PaxDb; 246196-MSMEI_2432; -.
DR GeneID; 66733904; -.
DR KEGG; msm:MSMEG_2491; -.
DR PATRIC; fig|246196.19.peg.2457; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 7055905at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000000757; Chromosome.
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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 181..284
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 390 AA; 39874 MW; 14C53503DD2E6B25 CRC64;
MGISAYEQAV LDRLDETLMV DLTVALVRSA GENPPGEEAA TVRTLADAAA ALDLEVDETQ
VEPGRDNISV TLNGGSGPGL LMLGHTDVVP AGTGWTTDPF GGVLRDGRIY GRGTSDMKGG
LAAALAAMAA LRGAGLSGPV ELAALVDEEE NGKGIRAYVD AVHRNYLGCI TAEPTDLQTI
IGARGASYVR VEIHGKACHA GNPDDGANAI YGAAAAIAEI ERLHRELARQ PHPLLGAATW
SVGQVHGGTA GAIVPDECVL VADRRLLPGE SGADVVDGLR TRLTGLADRG LSVDVSMPME
MPPFQTPADA DLVLTAESAL ADAGGPGLPV GGWTAACDGG FIARDLGVPV VVLGPGSVTE
QAHRADESVA VEQLLVAARA YVLTALRLLG
//
