ID A0A1G7KYY4_9RHOB Unreviewed; 387 AA.
AC A0A1G7KYY4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN04489759_102162 {ECO:0000313|EMBL:SDF42413.1};
OS Sulfitobacter delicatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=218672 {ECO:0000313|EMBL:SDF42413.1, ECO:0000313|Proteomes:UP000199399};
RN [1] {ECO:0000313|EMBL:SDF42413.1, ECO:0000313|Proteomes:UP000199399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16477 {ECO:0000313|EMBL:SDF42413.1,
RC ECO:0000313|Proteomes:UP000199399};
RA de Groot N.N.;
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}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691}.
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DR EMBL; FNBP01000002; SDF42413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7KYY4; -.
DR STRING; 218672.SAMN04489759_102162; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000199399; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03894; M20_ArgE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010169; AcOrn-deacetyl.
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 NCBIfam; TIGR01892; AcOrn-deacetyl; 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 SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 173..286
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 387 AA; 42247 MW; 0845C848E9C44BAF CRC64;
MTPRMTPLEL MTKLISFPTV SRDTNIPLID WVAEYLSSHG IESHRYIDPE QPKHALFAHA
GPWEEGALVL SGHTDVVPID GQPWESDPFT VTERDGRYYG RGTCDMKGFD ALAIWALVEA
HYAQVKRPLQ IALSFDEEVG CTGAPPMIQA MQGVVPKGSA VIVGEPSTMQ AVTGHKGGIG
FNTHLVGFEV HSSLLHTGVN AIMAGAKLIE WANDVNSDNM AAKPTETAAM FDPPFTTAHV
GVIEGGTAHN ITAKDCKFAM DFRVVPGEDK DKWGTAYLKK VREVEKQMQA IVPETYIETS
TRFDVPALQP EKEGEAEQIV RQITGDNASH KVSYGTEAGQ FQEAGYSAVI CGPGDIAQAH
QPNEYIEVAQ FEAGHDFMRK LVTRLQG
//
