ID   A0A0Q5UY68_9SPHN        Unreviewed;       414 AA.
AC   A0A0Q5UY68;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQS49318.1};
GN   ORFNames=ASG20_09865 {ECO:0000313|EMBL:KQS49318.1};
OS   Sphingomonas sp. Leaf198.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS49318.1, ECO:0000313|Proteomes:UP000050871};
RN   [1] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA   Garrido-Oter R.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS49318.1}.
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; LMPX01000002; KQS49318.1; -; Genomic_DNA.
DR   RefSeq; WP_056051520.1; NZ_LMPX01000002.1.
DR   AlphaFoldDB; A0A0Q5UY68; -.
DR   STRING; 1736299.ASG20_09865; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000050871; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03886; M20_Acy1; 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:KQS49318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050871}.
FT   DOMAIN          206..298
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   414 AA;  43569 MW;  24C4366F26F9A10E CRC64;
     MSLDFESTTD WAPTDWTAVG EDSLDDAITL RRAIHADPEV GLHCPRTSDK VKAALAGLPL
     EIRGGTSTTG FVAILRGGRG GNAGGNGRTV LLRGDMDALP MQEETGLPFA SKIDGAMHAC
     GHDSHTAMLV GAAKALCARR DELPGTVVFM FQPGEEGHHG ARHMIADRLL DSPLPEAGFA
     LHISPNMPMG HVVSRAGTLM ASTDTLRATI TGRGGHAAMP HDCLDPLPIA CEIVTALQTY
     VARQVAVTDP AVLSITKLNA GSAHNVIPSS VEMLGTMRTL SERTREQVRA AFIRMVEGIA
     AAHGAVGTPT IEEGYPVTVN DERATDLMKA CATAIGGEGA YQVMPPMMGA EDFSYVLQKL
     PGAMAFIGAA PEGSDPRTNP PLHNTKMTID ERVMAHGIAM HCAVAERFLA NGFG
//