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Database: UniProt
Entry: A0A0S8BC08_9BACT
LinkDB: A0A0S8BC08_9BACT
Original site: A0A0S8BC08_9BACT 
ID   A0A0S8BC08_9BACT        Unreviewed;       559 AA.
AC   A0A0S8BC08;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=AMS20_01040 {ECO:0000313|EMBL:KPK09128.1};
OS   Gemmatimonas sp. SG8_28.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK09128.1, ECO:0000313|Proteomes:UP000051120};
RN   [1] {ECO:0000313|EMBL:KPK09128.1, ECO:0000313|Proteomes:UP000051120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_28 {ECO:0000313|EMBL:KPK09128.1};
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:KPK09128.1}.
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DR   EMBL; LJNQ01000007; KPK09128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8BC08; -.
DR   PATRIC; fig|1703357.3.peg.558; -.
DR   Proteomes; UP000051120; 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: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.
PE   4: Predicted;
FT   DOMAIN          64..552
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   559 AA;  62037 MW;  15F7F2C985A9313B CRC64;
     MACAPRAGEG AVVYTAKKII TMEEATPEAT AVAVAHDRIV AVGSLEEVRQ QLDGQPYDVV
     DTFEDKVLVP GFIDNHMHPL LVGGFLLQAD FITPFDWTLP SQQVEGVQGR DAYLARLQEI
     EAAKTDPEDW LLTWGHSPAF HGEVWRADLD EISSTRPILV WARSFHEVTL NTAALEALGF
     LSGDDPQHHQ IHYDKGWFLE TGYKSYLLPK MAGILLEPER LMPALKEAGE ALHLGGITTV
     ADMAAGAMDP ETEVNSAVAA YENDSTPFRA FYVPVGSEVV TDRYGGLEQG AEFYAGLPEM
     NTHRIQWVKQ VKFLADGAFY SQLMQMQDGY TDGHSGEWIM PPDELERAAR VFWNRGWQIH
     VHVNGDLGMQ VTLDVLEKLQ QENPRDDHRF TLHHTGYFTA EQARRIAELG ALVSAQPFYL
     YALGDKYSEI GLGPERAHYM VRLKSLLDSG VKVSLHSDFT MAPAEPLRLA WVAVNRLSAS
     GEVLGPEERI TVEQALRAIT IDAAYAIRME DEIGSIAPGK IADFAVLEQD PYEVPPAQLK
     DIPIWGTVFE GKLFPIGEN
//
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