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Database: UniProt
Entry: A0A101E927_9FIRM
LinkDB: A0A101E927_9FIRM
Original site: A0A101E927_9FIRM 
ID   A0A101E927_9FIRM        Unreviewed;       398 AA.
AC   A0A101E927;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KUK10485.1};
GN   ORFNames=XD50_1237 {ECO:0000313|EMBL:KUK10485.1};
OS   Clostridia bacterium 41_269.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK10485.1, ECO:0000313|Proteomes:UP000053409};
RN   [1] {ECO:0000313|Proteomes:UP000053409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK10485.1}.
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DR   EMBL; LGEZ01000013; KUK10485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101E927; -.
DR   STRING; 1635275.XD50_1237; -.
DR   PATRIC; fig|1635275.3.peg.955; -.
DR   Proteomes; UP000053409; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01309; Met_dep_hydrolase_C; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KUK10485.1}.
FT   DOMAIN          287..389
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   398 AA;  43603 MW;  CC08644FCA94452E CRC64;
     MFALVNGRIL TVYCHREKPS SEGEFPVYDP GWIAVSDSKI YAVGPGLNPS IKCSEVIDLK
     GKVVTPGLID AHTHLGIYEE GKSKEGDDTN EISSPVMPHL RAIDAINPRD IGFRSARENG
     ITCVCCLPGS SNVVGGLGVV LKTAGDIVDT MVIRDNAGLK VAFGENPKKE YGNRKKSPAT
     RMAIAALLRE SFIQAVHWKE EKDRRAFGTE DIKNEIFVKV LKGEIPLRVH AHRADDIMTA
     IRIAEEFHLP IVLDHCTEGH FVASEIAKRG IPVVYGPMLL GKVKQELGEL TEKTPAVLFK
     AGVRFALTTD HPEISIKHLM LCAALSVREG LPKEEALKAV TFNAAEILGL SHRIGSLWPG
     LDADIVVWSG DPFDITSRVE MVWINGRMVY NASDDKLQ
//
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