ID F8NB73_9BACT Unreviewed; 350 AA.
AC F8NB73;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=Premu_0409 {ECO:0000313|EMBL:EGN55891.1};
OS Hallella multisaccharivorax DSM 17128.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN55891.1, ECO:0000313|Proteomes:UP000002772};
RN [1] {ECO:0000313|Proteomes:UP000002772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX PubMed=22180809; DOI=10.4056/sigs.2164949;
RA Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Ivanova N.;
RT "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT Prevotella multisaccharivorax type strain (PPPA20).";
RL Stand. Genomic Sci. 5:41-49(2011).
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}.
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DR EMBL; GL945017; EGN55891.1; -; Genomic_DNA.
DR RefSeq; WP_007572717.1; NZ_GL945017.1.
DR AlphaFoldDB; F8NB73; -.
DR STRING; 688246.Premu_0409; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_10; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000002772; 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 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, ECO:0000313|EMBL:EGN55891.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002772};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 167..269
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 350 AA; 39105 MW; BD800EA252AFA001 CRC64;
MRQKDYVGDA IELLRQLIAT PSISRGERAA ADILGQHIIS YGMKLRREGN NIWALSPDWD
EAKPTLLLNA HIDTVKPVES WTRDPFQPMI ENDCLYGLGS NDCGGGLTTL LQVFRWLTLR
PQPYNYIYLA SAEEEVSGKN GIAKVIPLLP KIDVAIVGEP TGMQPAIAER GLMVLDLIAH
GKSGHAARNE GVNAIYEALD DMQWIRDYRF EKVSPLLGSV KMTLTAVNAG TQHNVIPDRC
TMLVDVRTNE RYTNEEVFDI ISKHVKSEVH AHSFRLHSSH ISSDHPLIRR CVALGMKPYG
SPTLSDQALM PWPSFKLGPG ESSRSHSADE YIHVSEMQQA FYTYLKILEG
//