ID A0A086YVV2_9BIFI Unreviewed; 407 AA.
AC A0A086YVV2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=BACT_0308 {ECO:0000313|EMBL:KFI38402.1};
OS Bifidobacterium actinocoloniiforme DSM 22766.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI38402.1, ECO:0000313|Proteomes:UP000029015};
RN [1] {ECO:0000313|EMBL:KFI38402.1, ECO:0000313|Proteomes:UP000029015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI38402.1,
RC ECO:0000313|Proteomes:UP000029015};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00001246};
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; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}.
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:KFI38402.1}.
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DR EMBL; JGYK01000004; KFI38402.1; -; Genomic_DNA.
DR RefSeq; WP_033504861.1; NZ_JGYK01000004.1.
DR AlphaFoldDB; A0A086YVV2; -.
DR STRING; 1437605.AB656_00095; -.
DR KEGG; bact:AB656_00095; -.
DR PATRIC; fig|1437605.7.peg.19; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 7055905at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000029015; 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 GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 InterPro; IPR001160; Peptidase_M20C.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PRINTS; PR00934; XHISDIPTASE.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI38402.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 171..277
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 407 AA; 43982 MW; 5C131683DA1FDE95 CRC64;
MTNEEKLELL RKLVAFQSVN GHELPVAEFI KSLLAKEGIE SEIVPTGEDR ADLVASIGSG
HPVLAISGHM DVVDVDRGNW KTDPFVLTQA DDGDSLYGRG ATDMKSGLAA MIISMIELKR
EDAPLKGTLK FLVTSGEEVG QEGAEILQRK GYMKGVDALL IGEPSGYLAV YANKGELDLT
IKAQGRAAHS SIPALGVNAV EALLQVLDQI KERMAQASAS ANNDVLGGTV FNIDTIRGGN
QVNAIPANAE AEINIRTIPE FDNEVILKTI NEVIDSFNAS SQAHVSMDVD MDIVPIIGNV
DSKLIKLAQE VAKPYMAKVE WTEEGERKAR ALSKAVGAPF SKTDLVTLGV SGGTDGSKFL
IDQPIGFDYL MFGPGSGTQH QDNEWVSKAM YLDFTHLYKE LFKRYLS
//
