ID A0A117LD48_9BACT Unreviewed; 389 AA.
AC A0A117LD48;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=XD68_1083 {ECO:0000313|EMBL:KUK39353.1};
OS Synergistales bacterium 54_24.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK39353.1, ECO:0000313|Proteomes:UP000054050};
RN [1] {ECO:0000313|Proteomes:UP000054050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:KUK39353.1}.
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DR EMBL; LGFQ01000045; KUK39353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LD48; -.
DR STRING; 1635272.XD68_1083; -.
DR PATRIC; fig|1635272.3.peg.1023; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000054050; 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; 2.
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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 183..286
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 389 AA; 41635 MW; 2EC0721686433AED CRC64;
MEYERLFSKV SEDELAKLCA ELVRFDTTNP PGNERAAAEW AARYLEDLGF EAEFVPHGES
RATLVAHLKG SGDVPPLAFN GHLDVVPAGA QEWKHPPFGG EISEGKVWGR GSSDMKGGIA
AMLVAAKAVA TSGLSLKGDL IFLATSGEEL DMMGAKSLTS RKDLAKAQAI IIAEPTDNEV
VLTERGVFWP EFTTYGKTAH GSTPELGHNA IKDMMALLLE LEKTEIPYEP HPVAGRFSMS
INTINGGVKT NVVPDKCVAT VDMRTVPGQD HEALLSQLDG IVKRLEAKIH NFKASIRITN
DLPPADTSPD EPVVKRFLEV AQSVAPGVKV GKAPFATEAA VFVPSMGVPT IIFGPGDPRL
AHQPDEYVEI SKMTTSARVF AAVASALLA
//
