ID A0A2P8DAM1_9BACT Unreviewed; 357 AA.
AC A0A2P8DAM1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=B0I18_101410 {ECO:0000313|EMBL:PSK94255.1};
OS Taibaiella chishuiensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Taibaiella.
OX NCBI_TaxID=1434707 {ECO:0000313|EMBL:PSK94255.1, ECO:0000313|Proteomes:UP000240572};
RN [1] {ECO:0000313|EMBL:PSK94255.1, ECO:0000313|Proteomes:UP000240572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12700 {ECO:0000313|EMBL:PSK94255.1,
RC ECO:0000313|Proteomes:UP000240572};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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 -!- 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:PSK94255.1}.
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DR EMBL; PYGD01000001; PSK94255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8DAM1; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000240572; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05651; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 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 SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000240572};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 169..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 357 AA; 38754 MW; A433B8DDD0D7D3A5 CRC64;
MNEQTQLYEE ALDLLRQMIR IPSFSREEAG TATLLENWLQ QRGIPASRAG NNVYARNLHF
DDGKPTLLLN SHHDTVKPAS GYTTDPFGAL IMDGKLYGLG SNDAGASVVC LTAAFRHFYA
MPDLPYNLIL ALTAEEEISG YEGIVALLPL LGRIDCALVG EPTQMQMAVA ERGLMVLDVT
VKGQSGHAAR NEGVNAIYEA LTAVTWFRNY HFPAASDLLG PVSMQVTSIH TDNKAHNVVP
DTCSFVVDIR INECYTHEAI LATVQQHVSG SITPRSTRLR SSNIAAQHPL VQAGAAMGLR
SYGSPTLSDK ALMPFPALKI GPGDSARSHT ADEYIRLDEL ASGIDQYISL LGRVPHL
//
