ID A0A1F6RYH8_9BACT Unreviewed; 525 AA.
AC A0A1F6RYH8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=A3J76_01135 {ECO:0000313|EMBL:OGI25721.1};
OS Candidatus Moranbacteria bacterium RBG_13_45_13.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1801635 {ECO:0000313|EMBL:OGI25721.1, ECO:0000313|Proteomes:UP000178026};
RN [1] {ECO:0000313|EMBL:OGI25721.1, ECO:0000313|Proteomes:UP000178026}
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:OGI25721.1}.
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DR EMBL; MFRT01000021; OGI25721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6RYH8; -.
DR Proteomes; UP000178026; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
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;
FT DOMAIN 45..506
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 525 AA; 58586 MW; 01B8929B504DA37A CRC64;
MYDILIKNGT VIDGTGKAGI PADVAISKNK IAKVGKIRWS KGRTEIDARG KIVCPGFIDV
HNHSDAYWQL FLEPTLPSLV HQGITTIIGG NCGTSIAPLA EGRVIESIQK WTDLREVNVD
WLSIEEFAEK LRARKMGLNF GTLVGHGTLR RGILHDEMRR LDRNELDEIE RILEIALFEG
ALGFSTGLAY SHEKSATWDE LVELAEIAKS QDRIYSTHLR DEAGEVASAL QEAIDLSKQT
GVSLQVSHLK VMGEKNWHLM DVVLSEIEKA HKAGVDINFD VYPYTQTGSV LYVYLPAWAA
EGGKRMLVKR LKEKHLRKKI IEEMRETAGY HYENAVIAVC SFSKSLSNRK IAEIASERGV
LAEEVIMDLL LASEGRVITI MECLGEENVK KAIKHPLSII ATDGAGYNVS RKESGELVHP
RCFGTFAKVL GKYVREEKLM SFEEAIKKMT SLPAKKFGIE GRGRLEKGKF ADITVFDPKI
VSDKATVENP YQYSDGIEQV ILNGKFLMRD MKLTGEMNGE FLMTN
//