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Database: UniProt
Entry: R5RYB3_9FIRM
LinkDB: R5RYB3_9FIRM
Original site: R5RYB3_9FIRM 
ID   R5RYB3_9FIRM            Unreviewed;       530 AA.
AC   R5RYB3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Amidohydrolase family protein {ECO:0000313|EMBL:CCZ45793.1};
GN   ORFNames=BN483_00934 {ECO:0000313|EMBL:CCZ45793.1};
OS   Firmicutes bacterium CAG:129.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263003 {ECO:0000313|EMBL:CCZ45793.1, ECO:0000313|Proteomes:UP000018410};
RN   [1] {ECO:0000313|EMBL:CCZ45793.1, ECO:0000313|Proteomes:UP000018410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:129 {ECO:0000313|Proteomes:UP000018410};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ45793.1}.
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DR   EMBL; CBAB010000093; CCZ45793.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5RYB3; -.
DR   Proteomes; UP000018410; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR023100; D-aminoacylase_insert_dom_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
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:CCZ45793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018410}.
FT   DOMAIN          45..487
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   530 AA;  56770 MW;  0B43EFA8895B0560 CRC64;
     MLDWLIRGAQ VLDGTGADAF PADVGIKDGT IAAVGRLTDV DAAHVLDAQG RTLTPGFLDI
     HRHTDAALFR PNFGRAELAQ GLTTLVGGNC GMSLAPLAGA HAPAVRSYLA PITGAFGDEL
     CFASLADYFA AAERTPQIVN NAMLAGMGTL RALVAGFDDA PLTDGQYREL HRLVERSLAD
     GAVGVSLGLG YAPECFYSTE GLIRALEPLR GGRLPVTVHM RQEGDGVVDA LREMLTVARE
     LRCPVEISHL KGIGRANWGR AVPEMLRLLE NARAEGLDVA CDVYPYSAGS TQLIHVLPPE
     FQKGGLDALT AALRDPGSRA AMRGRMETGS DFENITHLVG FENVVPISLH TEEYKPFEGK
     SLAEIADMLG KDPYDALFDL LAAERCEAGM IDFIAAEEDI EAILRAPFSV PISDATYPVE
     GLCHPRVYGS AARFLAHYVR ERGILTLPQA VHKLTMQSAD RLGLSRKGRI AVGADADLCL
     FSPENIRENG AYTAPRQLAS GMDAVFVAGV PEIMDGQFTG ETRGRVLRAH
//
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