ID F8GI20_NITSI Unreviewed; 509 AA.
AC F8GI20;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AEJ01469.1};
GN OrderedLocusNames=Nit79A3_1653 {ECO:0000313|EMBL:AEJ01469.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01469.1};
RN [1] {ECO:0000313|EMBL:AEJ01469.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01469.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002876; AEJ01469.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GI20; -.
DR STRING; 261292.Nit79A3_1653; -.
DR KEGG; nii:Nit79A3_1653; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_635861_0_0_4; -.
DR OrthoDB; 9782972at2; -.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AEJ01469.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..509
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003377666"
FT DOMAIN 98..419
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 509 AA; 53945 MW; CFFFDDDED57222E2 CRC64;
MRNGNRNFNK KHLVISLILW QGISCSVFAH EGEDHTGTAG APGLPDCQIL AAARLFDGIN
FPLDNMAVLI EGDKIKQVDT LTELSGLCAN QINLGDATIL PGFIESHAHI TFQNVNKNAV
LEHGITTVQD TGGPLMAPEG GQGTLRLLSA GPIIQAVDGY PLNIFGGGDG GYDKIGVHVA
STTEAEKVVT DLVAGGATAI KIALEPGGET GAPWMQPHDG PVPPTPWPML SQDITNAIVA
KAHALGKRVI VHAGENTGFE RALDAGIDEF AHIPCAEIND SLLQRAVDQG ITFVTTIDTL
ASCVDTATQK GIHSNTMSLA SKGAKFIYGS EIGHDNVPWG INGEEFHMML HLTSGASIDF
TDVVNVFKAA TSKAGEHLGF APLGTLVPGA PADVIAVQGN PFEKFKLLEY PSLVISGGRT
IVNKFINQSS AANVECFLTW AEGKYPDLFA PSGAATEVSS FYSYRYYAKT EAYLGISSTD
NHVYYMKKAD GVLQDEGSLS NWLPVSGCR
//
