ID A0A132PM00_9MYCO Unreviewed; 355 AA.
AC A0A132PM00;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=AFM11_16880 {ECO:0000313|EMBL:KWX23042.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX23042.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX23042.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX23042.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWX23042.1}.
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DR EMBL; LGTW01000010; KWX23042.1; -; Genomic_DNA.
DR RefSeq; WP_067850788.1; NZ_LGTW01000010.1.
DR AlphaFoldDB; A0A132PM00; -.
DR STRING; 59750.AWC31_01450; -.
DR PATRIC; fig|59750.3.peg.729; -.
DR Proteomes; UP000070612; 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: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:KWX23042.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070612};
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; 37111 MW; AFDAAADD5C1D9EEF CRC64;
MGLDLRADPI ALTAALVDIP SESRHEQRIA DEIEAALRAQ APAFEVIRNG DAVLARTNLG
RPSRVMLAGH IDTVPAADNL PSRVVDGEMY GCGTSDMKSG DAVFLHLAAT IAEPSHDITL
VMYDCEEIES SANGLGRIER ELPDWLVADV AILGEPSGGY IEAGCQGTIR VVVRAAGTRA
HSARSWLGDN AIHKLGAVLD RLSAYQARSV DIDGCVYREG LSAVRIDGGI AGNVIPDAAA
VTVNFRFAPD RSVDQAVAHV HEVFDGLDVT IELTDAAAGA LPGLSKPAAA ALIAAAGGQV
RAKYGWTDVA RFAALGIPAV NYGPGDPNLA HRVDERVPVA AITAATGMLR GYLTS
//