ID A0A1G1NAE2_9BACT Unreviewed; 259 AA.
AC A0A1G1NAE2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=CN hydrolase domain-containing protein {ECO:0000259|PROSITE:PS50263};
GN ORFNames=A3D10_06695 {ECO:0000313|EMBL:OGX26536.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_48_11.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801856 {ECO:0000313|EMBL:OGX26536.1, ECO:0000313|Proteomes:UP000176613};
RN [1] {ECO:0000313|EMBL:OGX26536.1, ECO:0000313|Proteomes:UP000176613}
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 -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000256|ARBA:ARBA00010613}.
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:OGX26536.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHGP01000047; OGX26536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1NAE2; -.
DR STRING; 1801856.A3D10_06695; -.
DR Proteomes; UP000176613; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 1..243
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 259 AA; 28522 MW; E1DFB2529578C74A CRC64;
MGAGPDKAHN VAKAVYLVEQ AVRGHAEFVL LPEMFNYRGT MSAQSVLNTY KEKIPGESIQ
PFMDLAKKHK ISILAGSICE EIPHSDKVYN ASVLIDEQGM ISATYRKMHL FDAQLGTTAV
KESLSFVAGQ QPVTAKVGEF TVGLSVCYDV RFPDLYQTYA RQGAQLLTVP SAFTKTTGQA
HWEVLLRARA IENLCYVLAP NQIGKDGRGV EAYGHSMIVN PWGEILAVAS ADREEIITAE
LERNVLLEKR KILPGINKI
//
