ID   A5PDJ2_9SPHN            Unreviewed;       458 AA.
AC   A5PDJ2;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   13-SEP-2023, entry version 47.
DE   SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:EDL47995.1};
GN   ORFNames=ED21_29151 {ECO:0000313|EMBL:EDL47995.1};
OS   Erythrobacter sp. SD-21.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL47995.1, ECO:0000313|Proteomes:UP000005498};
RN   [1] {ECO:0000313|EMBL:EDL47995.1, ECO:0000313|Proteomes:UP000005498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD-21 {ECO:0000313|EMBL:EDL47995.1,
RC   ECO:0000313|Proteomes:UP000005498};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDL47995.1}.
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; ABCG01000008; EDL47995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5PDJ2; -.
DR   STRING; 161528.ED21_29151; -.
DR   eggNOG; COG1473; Bacteria.
DR   Proteomes; UP000005498; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:EDL47995.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005498};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..458
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002687180"
FT   DOMAIN          231..327
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   458 AA;  48875 MW;  F17DD1069FAB9CCA CRC64;
     MFHLFHPEGE PEPMSNLRPT FVLTACALAA SAFAAPASAN DLRASLEEDM PGLMELYRDL
     HAHPELSFEE HKTAAKLAAR MRALGFEVTE GVGQTGVVSV MKNGEGPTVL LRADMDGLPV
     IEQTGLPYAS KETATPASGV TTGVMHACGH DTHMAGFIGA AQLLAERKDE WQGTLVMILQ
     PAEELGLGAL AMLEDGLYTR FPKPDYAIAF HDAAAPAPAG TIGFTPGYAL ANVDSVDILV
     KGVGGHGAYP HTTRDPVVLA SAIVMKLQTI VSRNSSPLDP AVITVGSFHA GAKHNIISDE
     AKLQLTVRSY SDESRKLLLD GIRRVARGEA ITAGLPEELY PVVTVEEPYT PSTFNDPDFS
     EQLAAGFRER FGEARVMQWP AVMGGEDFSQ FRRAAPEDVK SMIFWISGTP APMLKALKEE
     GKPLPSLHSP FWAPDAEAVV KTGAEALASA ALDLMPAP
//