ID Q12DM1_POLSJ Unreviewed; 423 AA.
AC Q12DM1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN OrderedLocusNames=Bpro_1422 {ECO:0000313|EMBL:ABE43371.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE43371.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CP000316; ABE43371.1; -; Genomic_DNA.
DR RefSeq; WP_011482370.1; NC_007948.1.
DR AlphaFoldDB; Q12DM1; -.
DR STRING; 296591.Bpro_1422; -.
DR KEGG; pol:Bpro_1422; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_3_4; -.
DR OrthoDB; 7055905at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd02697; M20_like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
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; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 207..315
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 423 AA; 45838 MW; 3C6C1FE151974425 CRC64;
MTTNTNTDTN TNSDTAYKQL DRWIDDHFDE EVRFLQELIR VPTDTPPGNN APHAERTAEL
LQAFGFEAEK HPVPEADVRA YGLESITNLI VRRRYSKPGE GRTIALNAHG DVVPPGEGWT
KDPYGGEIED GRIYGRAAAV SKCDFASFTF AVRALEALGA PLKGGVELHF TYDEEFGGEM
GPGWLLRQGL THPDLMIAAG FSYEVVTAHN GCLQMEVTVH GKMAHAAIPD TGVDALQGAV
HILNALYAQN ALYRKVTSGV AGISHPYLNV GRIEGGTNTN VVPGKVTFKL DRRMIPEENP
VEVEATIRQV IADAAAGCAG ITVNIKRLLL ANSMKPLAGN MPLVDAIQKH GEALFGQKIP
AMGTPLYTDV RLYAEAGVPG VIYGAGPRTV LESHAKRADE RLELEDLRRA TKVIARTLVD
LLA
//
