ID A0A1F3LXF6_9BACT Unreviewed; 417 AA.
AC A0A1F3LXF6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Chlorohydrolase {ECO:0000313|EMBL:OFY45127.1};
GN ORFNames=A2X18_14450 {ECO:0000313|EMBL:OFY45127.1};
OS Bacteroidetes bacterium GWF2_40_14.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797347 {ECO:0000313|EMBL:OFY45127.1, ECO:0000313|Proteomes:UP000176561};
RN [1] {ECO:0000313|EMBL:OFY45127.1, ECO:0000313|Proteomes:UP000176561}
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:OFY45127.1}.
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DR EMBL; MEOK01000001; OFY45127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3LXF6; -.
DR STRING; 1797347.A2X18_14450; -.
DR Proteomes; UP000176561; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01298; ATZ_TRZ_like; 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; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 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:OFY45127.1}.
FT DOMAIN 47..393
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 417 AA; 46925 MW; 536A17F0A21F7C89 CRC64;
MKSILIKNIV LNNKLTDILI KDNLIDKISE DIDFQADRII NGNGRSVIPG LVNMHTHAAM
TLMRGIGEDL SLTEWLESKI WPTERKLTDE MVYWGTKLAC LEMIKSGTTC FNDQYWSLPY
AVQAADEMGM RSFQPYVILD LLDESNSEKI KYECEKMYEL SGKWSSRNKF AIGLHAPYSV
SRNMIVWASE FAQKRDMLVH IHLSETKGEN DRSLAMHGVS STYYLEQLGV LNSKMIAAHC
LWMDDADIDL LAKRDVKIVH NINSNLKIAS GYKFRYNEFR DAGLTVSLGT DGCASSNNLD
MIETMKTTAL VQKGWRGDPR ELPLDELISL ATVNGGKSLG IKCGVIEEGY LADLVIIDTN
SVAFTPNINF LANLIYSANS SCVDTVICDG KILMENRIIE GEQEILRMAN KLYMDLL
//
