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Database: UniProt
Entry: A0A142EKY8_9BACT
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ID   A0A142EKY8_9BACT        Unreviewed;       568 AA.
AC   A0A142EKY8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AMQ55793.1};
GN   ORFNames=AO498_05180 {ECO:0000313|EMBL:AMQ55793.1};
OS   Algoriphagus sanaruensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ55793.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMQ55793.1, ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|EMBL:AMQ55793.1,
RC   ECO:0000313|Proteomes:UP000073816};
RX   PubMed=27174266;
RA   Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA   Shintani M.;
RT   "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT   Brackish Lake.";
RL   Genome Announc. 4:0-0(2016).
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DR   EMBL; CP012836; AMQ55793.1; -; Genomic_DNA.
DR   RefSeq; WP_067544463.1; NZ_CP012836.1.
DR   AlphaFoldDB; A0A142EKY8; -.
DR   STRING; 1727163.AO498_05180; -.
DR   KEGG; alm:AO498_05180; -.
DR   PATRIC; fig|1727163.4.peg.1078; -.
DR   OrthoDB; 9767366at2; -.
DR   Proteomes; UP000073816; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AMQ55793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073816};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..568
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007494001"
FT   DOMAIN          72..565
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   568 AA;  62376 MW;  CAD5FA955E0AE9F7 CRC64;
     MKNIYFLLIL ALFAGACTSG PENPVDSVYI NGIIYTVDEA NPQVQAVAVK DGLILAVGST
     EEIQAYVGEA TEVIDLQGKT MTPGFIESHA HLMGIGYNKL EIDLMGVKTY DELIQKVAEA
     AATAKPGDWI TGRGWHQDKW LQMPEKTVKG FQTHDALSAV TPNNPVYLAH ASGHASFVNQ
     KAMELAGITP LRSEKPTQEV EGGEVLRDEL GNPTGVLVER ASALVAKLIP ETTPEKNEEA
     LTLALQELAE KGITSFHDAG SGQEVIDLVQ KFKNEGKLTS RMYIMLTGRQ PELLEAWYKK
     GPMIDPDHFL TVRSIKLNCD GALGPWGAWL LEDYSDKPGH RGHETLPMSV VTEVSEKALP
     LGFQVCSHAI GDRANQEILD RYEAAFAKNP EAKDHRFRIE HAQHLHPDDI PRFGQLGVIA
     AMQAIHLSSD RPWAIDRLGE KRIIDGAYVW QSLFKTGALI ANGTDAPVEP VDPIPSFYAS
     VTRKTLQGLP EGGYEGEQKM TREQALKSYT LDGAFAEFEE NFKGSIEVGK AADFTVFDKN
     IMQIPEDEIL QTKVQMTVVG GEVVFSKQ
//
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