ID A0A1F4BEL5_9PROT Unreviewed; 413 AA.
AC A0A1F4BEL5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OGA22853.1};
GN ORFNames=A3I02_00235 {ECO:0000313|EMBL:OGA22853.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_02_FULL_67_26.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797492 {ECO:0000313|EMBL:OGA22853.1, ECO:0000313|Proteomes:UP000178840};
RN [1] {ECO:0000313|EMBL:OGA22853.1, ECO:0000313|Proteomes:UP000178840}
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:OGA22853.1}.
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DR EMBL; MERD01000076; OGA22853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4BEL5; -.
DR STRING; 1797492.A3I02_00235; -.
DR Proteomes; UP000178840; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01293; Bact_CD; 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 PANTHER; PTHR32027:SF9; BLL3847 PROTEIN; 1.
DR PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR Pfam; PF07969; Amidohydro_3; 2.
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:OGA22853.1}.
FT DOMAIN 45..132
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 165..399
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 413 AA; 44664 MW; 9D3C1084A8C2E8B1 CRC64;
MAFDLILRNA RLANGDAARA GVDIAIAEGR IAAIAPRVSG DGESVDAGGR FVSPGLVESH
FHLDKARILE RCAPPRDRRA GDHMKRTSAI KHTFTVEDVY ARARDTLEQC LLNGVTHMRT
HVEVDPNVGL RGFDAIERLA RDYAWGIDLQ LCVFLQEGWT NVEGGEANIA AALKRGARVV
GGAPRYDPDR PGQIRRIFAL AKEFDVDVDI HLDGGHTTHD MDIFLVCELT DRMGWGGRVA
IGHGAKYSCL PPAELDALGR RLAASGVAVT VLPATDLFNN GLHMEHSVLR GVADANALIA
QGANCSIATN NVMNPFTPYG DCSLVRIANL YANIVQRGSE ADLSECFAML TGRPARILRR
QDYGIAAGHP ADLVVWNAKT PAEVIATVAQ PVMGFKRGRR LFTREIAKLL GPA
//
