ID A0A1F5CVN8_9ARCH Unreviewed; 437 AA.
AC A0A1F5CVN8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=A3K70_01125 {ECO:0000313|EMBL:OGD46907.1};
OS Candidatus Bathyarchaeota archaeon RBG_16_48_13.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797381 {ECO:0000313|EMBL:OGD46907.1, ECO:0000313|Proteomes:UP000176610};
RN [1] {ECO:0000313|EMBL:OGD46907.1, ECO:0000313|Proteomes:UP000176610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD46907.1}.
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DR EMBL; MEZH01000001; OGD46907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CVN8; -.
DR STRING; 1797381.A3K70_01125; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000176610; 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; 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 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 217..325
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 437 AA; 47419 MW; 1377F18ED693DB62 CRC64;
MAVDQGKIVA LAKRALFRPV AVRNAFTQTA VHSSRGGSLL ASEISDILKR IDRKEVIELT
QELVRIPSVT GCEGDVAEYI QGRLKAFGLK TEKQNIVEKR FNVIGRMDGA SSENSLMLHG
HMDTVPTFDM EEPYSGKIIG DSIYGRGACD QKGGIAASMI ALKAIRESGL KLKKGILFAG
VIDEEAEHRG SYHLAKKGPR AEMAVITDQS NLEAEIGCKG SIPIRITTKG KAVHGSTPWL
GINAISKMVK IIEVMNQLSL GETKIEGLGN FKTTINIGLI QGGNAYNIVP DKCSIWIDLR
VVAGDDNQTI LKQFKEALRQ LKLKDKEIDA TMEVARPDWK WATILRRGLK PFLVPQDSSV
VVSLSEAIAA TGGKLRLSYS NGYVDADFLV NDASIPSVVY GPGGEGNAHS PKERVKIDQL
VQAAKVYAYM AAKEASK
//
