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Database: UniProt
Entry: D1Q0F2_9BACT
LinkDB: D1Q0F2_9BACT
Original site: D1Q0F2_9BACT 
ID   D1Q0F2_9BACT            Unreviewed;       356 AA.
AC   D1Q0F2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   Name=argE {ECO:0000313|EMBL:EFA42937.1};
GN   ORFNames=HMPREF0645_2687 {ECO:0000313|EMBL:EFA42937.1};
OS   Hallella bergensis DSM 17361.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA42937.1, ECO:0000313|Proteomes:UP000003160};
RN   [1] {ECO:0000313|EMBL:EFA42937.1, ECO:0000313|Proteomes:UP000003160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA42937.1,
RC   ECO:0000313|Proteomes:UP000003160};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (OCT-2009) 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:EFA42937.1}.
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DR   EMBL; ACKS01000108; EFA42937.1; -; Genomic_DNA.
DR   RefSeq; WP_007175082.1; NZ_GG704783.1.
DR   AlphaFoldDB; D1Q0F2; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_0_10; -.
DR   OrthoDB; 9792335at2; -.
DR   Proteomes; UP000003160; Unassembled WGS sequence.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:EFA42937.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003160};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          172..272
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   356 AA;  39677 MW;  A03570AE48C3990D CRC64;
     MERREQYTQD AITLLCRLVA TPSVSRSESE AATIMEQTIA GYGFETHREA NNLWVVDPWF
     DDARPTVLLN AHIDTVKPVK SWQHDPFIPT IEGDMLYGLG SNDCGGGLVT LLQVFRRFCT
     DAARSHRAFN LIYLASAEEE VSGKNGISRV LPRLPKIDVA IVGEPTGMQP AVAEKGLMVL
     DLKAHGKSGH AARNEGVNAI YEALEDMQWI RNYRFKKTSR LLGSVKMSLT MVNAGTQHNV
     IPDTCSMVVD IRTNECYTNE EVYNIVCRHV KSEVSARSFR LHSSHIDLEH PLVRRCVSLG
     MTPFGSPTLS DQSLMPFPSL KLGPGESSRS HSADEYIRIS EIEHAFDTYV KLLGMP
//
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