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Database: UniProt
Entry: E6WP31_PSEUU
LinkDB: E6WP31_PSEUU
Original site: E6WP31_PSEUU 
ID   E6WP31_PSEUU            Unreviewed;       440 AA.
AC   E6WP31;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADV25930.1};
DE            EC=3.5.1.47 {ECO:0000313|EMBL:ADV25930.1};
GN   OrderedLocusNames=Psesu_0067 {ECO:0000313|EMBL:ADV25930.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV25930.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV25930.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002446; ADV25930.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6WP31; -.
DR   STRING; 743721.Psesu_0067; -.
DR   KEGG; psu:Psesu_0067; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_6; -.
DR   Proteomes; UP000008632; Chromosome.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:ADV25930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..440
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003214873"
FT   DOMAIN          231..326
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   440 AA;  46444 MW;  8E7D1026AC06C098 CRC64;
     MPCKPLMHSL ALACLLALGA TAPADAAAPR PEVDAAAAKL QAQVVHWRRD FHQHPELSNR
     EQRTGQVIAR ELAKMGLEPR TGVAGHGVVA VLKGGRPGPR IALRADMDAL PVTERNDLPF
     ASKATGEYRG QKVGVMHACG HDAHMAILLG VARALVDRRA QLPGEVMFVF QPAEEGAPPG
     EQGGAPLMLE QGLFDGFRPE AIFGLHVFSS VQAGKIAVRG GPLMAASDRF GIKVIGRQTH
     GSRPWGGIDP VVAAADIVGS AQSIVSRRTD IARLPAVVTF GAINGGVRYN IIPDEVEMVG
     TIRTFDPGMR EAILADLRNV ASHVAAAHGA RVEAQVPDGE GNPATVNDPE LTARMLPSLQ
     AAVGAENVYE PALQMGAEDF AYYAKEVPAM FFFVGATAPG IDPETAPGNH SPEFMLDETS
     LDVGLRALLQ VSLDYLHGPG
//
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