ID A0A1B6BDN9_9FIRM Unreviewed; 401 AA.
AC A0A1B6BDN9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=F3D3_2469 {ECO:0000313|EMBL:GAU77840.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU77840.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU77840.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU77840.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:GAU77840.1}.
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DR EMBL; BDHH01000009; GAU77840.1; -; Genomic_DNA.
DR RefSeq; WP_069874224.1; NZ_BDHH01000009.1.
DR AlphaFoldDB; A0A1B6BDN9; -.
DR STRING; 1048380.F3D3_2469; -.
DR OrthoDB; 9792335at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000095197; 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 PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAU77840.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000095197};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 183..292
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 401 AA; 45031 MW; A0CCE83D6D9A6BE8 CRC64;
MKTLLSKIDW TVYYNPNEVY ELAQKLVQIP SHKDVPTRER DVALFIKTYC EQNGLQAKLS
VVEGERYNVY ITLKGNDSGK TLLFNGHTDT VPPYEMTVPP FEGMIKEGYL WGRGCNDMKG
ALAAMITAML AIKRSDYKLK GDIILAAVVG EEEQSDGTEQ LVLEGIKADG AIVGEPSNYE
YAIGHRGLEW LEFEFIGKAA HGGVPKEGIN AISMASKFIE AVERDLMPQI ELRTNAYMGP
SVMNFGKITG GTQPSTVADQ CFLQIDRRYV TGETVISVMR EYQEIIDQLK AEIPEFQCEM
KRMPSNMMKQ FDHMYHYTSP EEAIVKSVEK VLESHLTEKA MITRKRGWTD AATLSYYGKI
PTVITGPGDI KDSHTKAEKI SLKSLNDYVV LYAEIALDFL K
//
