GenomeNet

Database: UniProt
Entry: A0A087EA42_9BIFI
LinkDB: A0A087EA42_9BIFI
Original site: A0A087EA42_9BIFI 
ID   A0A087EA42_9BIFI        Unreviewed;       389 AA.
AC   A0A087EA42;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KFJ04643.1};
DE            EC=3.5.1.47 {ECO:0000313|EMBL:KFJ04643.1};
GN   ORFNames=BISU_0653 {ECO:0000313|EMBL:KFJ04643.1};
OS   Bifidobacterium subtile.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=77635 {ECO:0000313|EMBL:KFJ04643.1, ECO:0000313|Proteomes:UP000029055};
RN   [1] {ECO:0000313|EMBL:KFJ04643.1, ECO:0000313|Proteomes:UP000029055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11597 {ECO:0000313|EMBL:KFJ04643.1,
RC   ECO:0000313|Proteomes:UP000029055};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFJ04643.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JGZR01000003; KFJ04643.1; -; Genomic_DNA.
DR   RefSeq; WP_024462747.1; NZ_JGZR01000003.1.
DR   AlphaFoldDB; A0A087EA42; -.
DR   STRING; 77635.BISU_0653; -.
DR   eggNOG; COG1473; Bacteria.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000029055; Unassembled WGS sequence.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-EC.
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   InterPro; IPR023827; Peptidase_S8_Asp-AS.
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.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFJ04643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029055}.
FT   DOMAIN          190..286
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   389 AA;  41207 MW;  23773C2D7A01A361 CRC64;
     MSQRDLQQEL ESYAKWFHQH PEPSYREFET TGRIRQIFDE HGIEILDSGL KTGLVAVIQG
     EGAGAGEGHV VAVRGDIDAL PIAEQTGLPY ASLNEGYLHG CGHDYNMTTA IGAALIINER
     RKDFAGTIKV ILQPAEEVAA DKDTPTGSVA VLDTGVLADV EAFYGTHDTN EAEPGTVIIG
     SGPDSGAVDK FRITVHGRGT HAAHPEGGLN PIRPAVAIIE GIQSIAGQDV DPAHPRVVTV
     THVEAGSTWN VVPAQAFLEG TARTAFPEDR TVIHDRLQAV VDGVAAAYGV TADFEWEYGS
     PSVMNDPHWS ALAASTATDV GFTVAAPHPS LGGEDFSYYL QQAPGAFIHI GVGNADRPMH
     GPTFFPKLDA LASGADLLAT VALRTLKEL
//
DBGET integrated database retrieval system