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Database: UniProt
Entry: A0A1F8KFM4_9CHLR
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Original site: A0A1F8KFM4_9CHLR 
ID   A0A1F8KFM4_9CHLR        Unreviewed;       527 AA.
AC   A0A1F8KFM4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=A2X25_14095 {ECO:0000313|EMBL:OGN72546.1};
OS   Chloroflexi bacterium GWB2_49_20.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN72546.1, ECO:0000313|Proteomes:UP000178842};
RN   [1] {ECO:0000313|EMBL:OGN72546.1, ECO:0000313|Proteomes:UP000178842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGN72546.1}.
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DR   EMBL; MGMF01000023; OGN72546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8KFM4; -.
DR   STRING; 1797612.A2X25_14095; -.
DR   Proteomes; UP000178842; 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          50..524
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   527 AA;  58479 MW;  0ADFCB73E09E3A06 CRC64;
     MKKILYNARI NTLDIDLPNA SALVIENGKL VAVGDAEIIL TEFGNYPKQD MGGKFILPGL
     TDAHLHLQYY GMGLQKVDCE TRSLVECIQR VAKRVQETES GEWVLGHGWN QNNWAEGFGS
     SAMLDVISSI HPIYLTAKSL HAAWANSEAL KRAGISASTP DPENGRIVRD DKGEPTGILL
     EDAMYLVSQE IPEPEIETLA KILQQAQTEL WKMGLTGIHD FDRRNCFSAL QLIHSRGELG
     LRVLKNIPVE DLPHAIGMGL RSGFGDDYLR IGSLKLFADG ALGPHTAAML EPFVDESKNY
     GILNLDKEQI FEYGSKAVDN GFSLAVHAIG DRANHEVLDG FMQIRKYEKM KAYPHFRHRI
     EHVQLLHPSD TSRLAELDLI ASMQPIHAPS DLFMAEKSWG ERSAFSYAWR TQLDHGARLA
     FGSDAPVESP NPFWGLHAAV TRQRADGSPG ESGWYPEQRL TVEEALHGFT QGPAYAAGME
     NKSGKLREGF LADLIVLDQN LFECDPSELI NIKPLATMVG GEWVWEV
//
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