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Database: UniProt
Entry: E8T348_THEA1
LinkDB: E8T348_THEA1
Original site: E8T348_THEA1 
ID   E8T348_THEA1            Unreviewed;       406 AA.
AC   E8T348;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADU96053.1};
DE            EC=3.5.1.47 {ECO:0000313|EMBL:ADU96053.1};
GN   OrderedLocusNames=Theam_0079 {ECO:0000313|EMBL:ADU96053.1};
OS   Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Thermovibrio.
OX   NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU96053.1, ECO:0000313|Proteomes:UP000006362};
RN   [1] {ECO:0000313|EMBL:ADU96053.1, ECO:0000313|Proteomes:UP000006362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15698 / JCM 12110 / HB-1
RC   {ECO:0000313|Proteomes:UP000006362};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT   "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002444; ADU96053.1; -; Genomic_DNA.
DR   RefSeq; WP_013536839.1; NC_014926.1.
DR   AlphaFoldDB; E8T348; -.
DR   STRING; 648996.Theam_0079; -.
DR   KEGG; tam:Theam_0079; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_0; -.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000006362; Chromosome.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-EC.
DR   CDD; cd08014; 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:0000313|EMBL:ADU96053.1}.
FT   DOMAIN          196..291
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   406 AA;  45107 MW;  F0C243BFA47CD07A CRC64;
     MEELKELILR SSLEIKEELI RWRRHIHMYP ELSGREFNTA EFVAEKLKNF GVDEVIENFA
     GSTAVVATVK GEKPGGCVAL RADMDALPTE EKTGKPYASR IKGVMHSCGH DAHTAMLLGA
     AKVLCKLRKE FKGSVKLIFQ PCEERHDCKG AQWLVEHGVL ENPRVEAIFA LHVYPELPTG
     YVGTRFGPML ASADVFKVVV KGKSTHASRP HQGIDPVLIA AQTVNTLHHV VSRYVDPLEP
     AVLTVGKIRG GFAENIIPDE VEFEGTVRTL SHQVRDRIPK QMEQAVKGIA AAYGGECEFE
     FQWGTPPLIN DKETTAFAVE KMKELLGDER VVILEKPSMG GEDFSVYLKE VPGTFIRLGV
     RNEEKDTVYP LHNSRFDIDE DALPIGTAVE AYLAIAWLNR SPKLGK
//
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