ID A0A151BEU1_9ARCH Unreviewed; 417 AA.
AC A0A151BEU1;
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=AYL30_004870 {ECO:0000313|EMBL:KYH38398.1};
OS Candidatus Hecatellales archaeon B24.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia;
OC Candidatus Hecatellales.
OX NCBI_TaxID=1779369 {ECO:0000313|EMBL:KYH38398.1, ECO:0000313|Proteomes:UP000075493};
RN [1] {ECO:0000313|EMBL:KYH38398.1, ECO:0000313|Proteomes:UP000075493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B25 {ECO:0000313|EMBL:KYH38398.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
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:KYH38398.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LUCC01000024; KYH38398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BEU1; -.
DR STRING; 1779369.AYL30_004870; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000075493; 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 203..318
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 417 AA; 45087 MW; F9A1D5ECF502DB40 CRC64;
MNFPGSSEEA ERRILERLEN MRDNIVRLSS DLIRIPTVNP PGENYGEISS FLSKKMDEIG
LKVEVFQASE SKLKELGLKP PRPVVVGTLE AGKPEEALHF NGHYDVVPAG EGWTVEPFKP
TVRNGRLYGR GASDMKGGIA AMLAAVEAVR KERVNLRGDL KLSFVPDEEI GGQTGTGCLA
ELGLMEGKAA LIGEASGIDR VCVAHKGALW LEVAVKGEAA HTCMAHKAVN AVEKAAKIIV
ELGKLKEGFK AKATRTPMLS GHENPVINIG GVIRGGVKAN VVPELCVFTV DRRLIPEENV
EEAEAEIVGL IEEMGREDPQ LQAEVKRILH VEAAFTPENE KICRVLVEAA GKVTGVKPQI
SGLPVFTDMH FFSQHMPSAI YGPGVLEKVH AADEYVPVEE LVASAKVYAL TILKMLA
//
