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
//