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Database: UniProt
Entry: E0SGM5_DICD3
LinkDB: E0SGM5_DICD3
Original site: E0SGM5_DICD3 
ID   E0SGM5_DICD3            Unreviewed;       387 AA.
AC   E0SGM5;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Peptidase M20D, amidohydrolase {ECO:0000313|EMBL:ADM97674.1};
DE            EC=3.5.1.32 {ECO:0000313|EMBL:ADM97674.1};
GN   OrderedLocusNames=Dda3937_00819 {ECO:0000313|EMBL:ADM97674.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM97674.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADM97674.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADM97674.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
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DR   EMBL; CP002038; ADM97674.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0SGM5; -.
DR   KEGG; ddd:Dda3937_00819; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_6; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0047980; F:hippurate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd05666; M20_Acy1-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADM97674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT   DOMAIN          183..276
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   387 AA;  41615 MW;  FB9589C3EF0DCCF2 CRC64;
     MRMGISPALI AQAVEWRRKL HANPELGYHE RQTSEMVATL LATFGFQVHT GLADTGVVGT
     LENGPGPVIG LRADMDALPV TELSDLTYKS QRSGVMHACG HDGHTAMLLA AACHLSETRR
     FSGTVRVVFQ PAEENLGGAR RMVEEGLFTR FPMDDIYALH NWPGLPVGHV GLSSGAMMAS
     LDSFEIVLIG KSCHAAMPEN GADPIMAASQ LVLSLQTIPS RRLSPQSSAV ISITQIAGGE
     AINVIPEKVV LRGTLRCLQA SVREQVKALI AQFVAQIPEV FGVTGSIAYY PGYPVTQNDV
     RAAQAVREVA ETTFGASQVQ WEIAPSMASE DFACMLEHCP GAYFWLGADG ETPSRPLHNA
     CYDFNDALIP HGVAMWVALV ENRLPIG
//
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