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Database: UniProt
Entry: A0A151FDF4_9EURY
LinkDB: A0A151FDF4_9EURY
Original site: A0A151FDF4_9EURY 
ID   A0A151FDF4_9EURY        Unreviewed;       384 AA.
AC   A0A151FDF4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN   ORFNames=AYK18_00455 {ECO:0000313|EMBL:KYK38883.1};
OS   Theionarchaea archaeon DG-70.
OC   Archaea; Euryarchaeota; Theionarchaea.
OX   NCBI_TaxID=1803813 {ECO:0000313|EMBL:KYK38883.1, ECO:0000313|Proteomes:UP000075311};
RN   [1] {ECO:0000313|Proteomes:UP000075311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL   Submitted (FEB-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:KYK38883.1}.
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DR   EMBL; LSSB01000002; KYK38883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151FDF4; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000075311; 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   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: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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          180..291
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   384 AA;  41874 MW;  C2D1FEC2C7F58960 CRC64;
     MNLSAIDDLK PYAVGLAQQL IQFPTENPPG RDYHNCAEFL KKECETLGLE TEIVQVEATD
     RYNVLAWTST RKTDLHFHCH YDVVPAGHGW AYNPFSGSIV DGTLYGRGSS DMKGGIAAVF
     TALKAVQNLE DISISVSLTP DEETGGALGA EYVVKNQLVD TKMAVLPEPT GLKTMFNACK
     GALWVQVTVH GEAGHPSVKG LGVNAFDRMV VIASRLQKLK EIVEHKKSAL HSYPEGGEWA
     NLTLGGRCSS GEAVNAVPGQ ALFTIDRRTL PEEDLETAQQ EIRECIGKDA EITVLMEARP
     FHIDEQTDVC QLLNTASETV MRTSVNCALC PGFLDARHFV HAGIPCVTWG PGIYGNAHIS
     NEFIRIEDMM TAAKVFYVMA TTTT
//
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