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Database: UniProt
Entry: A0A0S8A037_9BACT
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Original site: A0A0S8A037_9BACT 
ID   A0A0S8A037_9BACT        Unreviewed;       390 AA.
AC   A0A0S8A037;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-JUN-2023, entry version 14.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KPJ91932.1};
DE   Flags: Fragment;
GN   ORFNames=AMS18_08375 {ECO:0000313|EMBL:KPJ91932.1};
OS   Gemmatimonas sp. SG8_17.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ91932.1, ECO:0000313|Proteomes:UP000051607};
RN   [1] {ECO:0000313|EMBL:KPJ91932.1, ECO:0000313|Proteomes:UP000051607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ91932.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ91932.1}.
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DR   EMBL; LJNM01000155; KPJ91932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8A037; -.
DR   PATRIC; fig|1703355.3.peg.603; -.
DR   Proteomes; UP000051607; 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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KPJ91932.1}.
FT   DOMAIN          1..379
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPJ91932.1"
SQ   SEQUENCE   390 AA;  42284 MW;  E89F385DF91B02BC CRC64;
     LANSKALALA GVTAATADPP GGTVVRYGDG RPTGILKDAA QDLVARVIPD RSEAELDRAL
     DAAAEHALAR GVTFVADMGT WEGLETYRRA RQRGRLPLRV YAVVPLATRQ RLKEFVDQHG
     RGDDRLFWGG LKGFVDGSLG STTAWFYQPY EDEPSTTGLM VTDTADLREG IIAGDRYGFQ
     LIVHAIGDRA NDWLLDAYAA TRAANGERDR RPRVEHAQHL SRAAIARFAE LGVVPSMQPY
     HAIDDGRWAE KRIGPERIKT TYAFRDLLAA DAQLAFGSDW TVAPIDPLLG IYAAVTRRTT
     DGATPDGWIP EQKIAVAEAV AAYTSGTAYS VYLDDVLGTL VPGKHADLVV LSEDIFAISP
     PEIEAVRVDL TIVAGEVMYE RQAKGGEPES
//
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