ID   A0A1M3DID4_9SPHN        Unreviewed;       479 AA.
AC   A0A1M3DID4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN   ORFNames=BGO24_11565 {ECO:0000313|EMBL:OJV34625.1};
OS   Sphingomonas sp. 67-36.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV34625.1, ECO:0000313|Proteomes:UP000183964};
RN   [1] {ECO:0000313|EMBL:OJV34625.1, ECO:0000313|Proteomes:UP000183964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=67-36 {ECO:0000313|EMBL:OJV34625.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV34625.1}.
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DR   EMBL; MKSU01000002; OJV34625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3DID4; -.
DR   STRING; 1895849.BGO24_11565; -.
DR   Proteomes; UP000183964; Unassembled WGS sequence.
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; 2.
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; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          357..456
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   479 AA;  52286 MW;  B6595B9B76E5339F CRC64;
     MAAEAARAPA ELHLTGVTVV DPRDGRKSPG MTVVIRAGRI AALVPDAQQL PANGAQRIDA
     RGKFVVPGYN DMHSHVLELD DPSGSLALML AEGVTGFRQM SGSPALLAKR RAGTLPIGAA
     APQLLQTPGA ILTPFNAATP DVAREEVRRQ KAQGADFVKM GFANPDSFFA AVNEGRRIGI
     PVLGHLQEGT DPVEATAAGF RSIEHLGPGS AVWVRCSHDE EELRAESYRR DVIKLPPFKI
     PFMERIIMKK FERMLVNPSA FSKEADVDRL RHASESFSSA RAEDMAGHFA EDGSWQCPTL
     VRLRTQTFAD APDYEHDEML HYLPRKSVRR WREVTDVWKA RPAEVRQTYR DVYPRQLALT
     KLLHDAGVRM IVGTDGGSYL GPGLTLKQEF RELADAGIEP LAILQMATVN AADYLDRRDA
     IGLVEPGYDA DLVLLDADPL ARVENLHAIT GVVRGGAYYS RRNLDALKDE VAAGGGYLG
//