ID A0A1S8FJM1_9BURK Unreviewed; 438 AA.
AC A0A1S8FJM1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:OOG44614.1};
GN ORFNames=B0B52_05690 {ECO:0000313|EMBL:OOG44614.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG44614.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG44614.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG44614.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:OOG44614.1}.
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DR EMBL; MUNO01000012; OOG44614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FJM1; -.
DR STRING; 1944133.B0B52_05690; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000218978; 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 Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218978}.
FT DOMAIN 197..325
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 438 AA; 47313 MW; 515EDCF37DCE9B4C CRC64;
MNNDSLLKRI ESKRADVVAL TQDLVRIPTI NPPGDAYEAC ARLLGERLKK RGFAVEYIRA
EGAPGDRDSH PRINVVARYE GKSAGECVHF NSHIDVVEAG SGWTVDPFGG EVKDGKVYGR
GTCDMKGGLA SSVIACEAIL EEGLAFPGAL EISGTVDEES GGFSGVGYLA ERGYFSRPRV
HHVIIPEPLG VDRICLGHRG VWWGEVETRG RIAHGSMPFL GDSAINHMSA FIHMLEMQLQ
PRLSQRHTAE PVEPPGARVS TLNINSLHGG QVEQLFSLDG RGRPTGDLPA PVVAHSCRAV
LDRRFIAEEN LEAVKAEIVA MLDELKQTRP GFDYGIKDIM SFVPTATPRE APVVLATARA
IARVLGREPS YISSPGTYDQ KHIVRTGKLD ACIAYGPGIL DLAHQPDEYV GIQELVDSAK
IMALAALSLT RGELAVSS
//
