ID A0A1I0QBI8_9BACT Unreviewed; 435 AA.
AC A0A1I0QBI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN05216290_2187 {ECO:0000313|EMBL:SEW24397.1};
OS Roseivirga pacifica.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1267423 {ECO:0000313|EMBL:SEW24397.1, ECO:0000313|Proteomes:UP000199437};
RN [1] {ECO:0000313|Proteomes:UP000199437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12402 {ECO:0000313|Proteomes:UP000199437};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOIR01000002; SEW24397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QBI8; -.
DR STRING; 1267423.SAMN05216290_2187; -.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000199437; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:SEW24397.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:SEW24397.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199437};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..435
FT /note="succinyl-diaminopimelate desuccinylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011509306"
FT DOMAIN 212..330
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 435 AA; 47026 MW; 31BEAB4264A593FF CRC64;
MKNRLFLLVT LFVFTSPFAF AQLDRTEKKL AEWVDANNND ALALLKQIVN INSGTMNFEG
VKAVADVLAP KFEALGMDVI WEEGSEFNRA GHLMAKIEGG KGPKILMIGH LDTVFEPDSP
NQEWRQIDDH TVAGPGIADM KGGDVIILQA LSALHAQGLL KDMNIGVIMT GDEELSGSPL
SASKAELVEA AKWADIALGF ENGDGNPATV NVARRSSSGW KLTVTGNAAH SSQVFKPEVG
AGAIYEASRI LYQFYEELSK EEFLTFNPGM ILGGTTVTYN ENENGGSAYG KDNVVSKDVT
VTGDIRCISP EQLTNAQKVM KAIVARNLPK TSATIEFSEG YPPFAPKDAN YDLMRQFSKV
SQDLGYGEVG PVNPADAGAA DISFTSEYIK MGIDGMGMSG KDDHTINETG DLRALPKQSK
RAAVLIYRLF KEVSK
//
