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Database: UniProt
Entry: A0A0F5ZSQ3_9GAMM
LinkDB: A0A0F5ZSQ3_9GAMM
Original site: A0A0F5ZSQ3_9GAMM 
ID   A0A0F5ZSQ3_9GAMM        Unreviewed;       563 AA.
AC   A0A0F5ZSQ3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=RN22_19260 {ECO:0000313|EMBL:KKD58791.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD58791.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD58791.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD58791.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-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:KKD58791.1}.
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DR   EMBL; LASY01000097; KKD58791.1; -; Genomic_DNA.
DR   RefSeq; WP_046306804.1; NZ_LASY01000097.1.
DR   AlphaFoldDB; A0A0F5ZSQ3; -.
DR   PATRIC; fig|1581149.3.peg.4960; -.
DR   OrthoDB; 9031471at2; -.
DR   Proteomes; UP000033732; Unassembled WGS sequence.
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; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 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;
FT   DOMAIN          78..560
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   563 AA;  61781 MW;  FE36EDA1D8F691E2 CRC64;
     MNKNKLFKLL PIAAILATAG CTKNNEVAGP EAVIYTNGDI LTMNKAAPNA EAVVVVGEDI
     VAVGSLSELQ KTWNNHTIFD LEGKTLMPGL VETHHHIMME AAMMDFLDMS YQAEPDFDKM
     MEIFAAGQPL AEDNAFMPGW VIGLGWDAGK HGRVPTLEER DALFPDTPVF VAMQGHGGWY
     NSKGMELKGI TKDKEPPRDS AYVKDENGEL TGEISGLYAV LEAIGSYPGP RLDTAVKATH
     KAASQGFTTV SDIGADNVDN LKVLSEASLD ENFNVRVAVG VTNADGYLDI LSNRADFETD
     KVWISQTKMW LDGAVHGGNI YTDLEYQNDA YKHNKLAPWG TQEMFNDVAW NSVLNGVNYS
     FHANGNLSLE MGLNAVEYAR ERAKAEGIDD TNFKGQAIHL SISTPEQYTR MAELGVDPTF
     IIGHTYWAGG QIMNQYFLKH AQEYMFRVNT AFEAGLPVSL HNDAPVTPAL PWLGIETSVT
     RVTEDGNLLN PSEAITVQQA LEAYTINGAI QFGVDDMTGS LEPGKRADMI VIDRNPLKVE
     PDTIRDTQVE TTIFEGRVVY ERS
//
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