ID V5XFP9_MYCNE Unreviewed; 355 AA.
AC V5XFP9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=D174_20830 {ECO:0000313|EMBL:AHC26847.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26847.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC26847.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26847.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
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; CP006936; AHC26847.1; -; Genomic_DNA.
DR RefSeq; WP_019510493.1; NC_023036.2.
DR AlphaFoldDB; V5XFP9; -.
DR KEGG; mne:D174_20830; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_1_0_11; -.
DR Proteomes; UP000018763; 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:InterPro.
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 InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR NCBIfam; TIGR01900; dapE-gram_pos; 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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHC26847.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018763};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 167..265
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 355 AA; 37057 MW; F58377D07E975B46 CRC64;
MGLDLRADPI TLTAALVDIP SESRHEQRIA DEIESALRAQ APHFEVIRSG NAVLARTNLG
RSSRVLLAGH TDTVPAADNV PSRRDGDLMY GCGTSDMKSG DAVFLHLAAT IAEPAHDLTL
VMYDCEEIES SANGLGRIER DLPAWLAADV AILGEPSGGF IEAGCQGTIR VVATAAGTRA
HSARSWLGDN AIHKLGAVLD RLSRYQARSV DIDGCVYREG LSAVRIDGGI AGNVIPDAAS
VTINFRFAPD RSVEQAVAHV HEVLAGLDVT CETTDAAAGA LPGLANPAAA ALVAAAGGQV
RAKYGWTDVS RFAALGIAAV NYGPGDPNLA HKVDEHVDIT AITATTETLR AYLTA
//
