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Database: UniProt
Entry: A0A1F5C9R1_9BACT
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ID   A0A1F5C9R1_9BACT        Unreviewed;       574 AA.
AC   A0A1F5C9R1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OGD39592.1};
GN   ORFNames=A2V45_12795 {ECO:0000313|EMBL:OGD39592.1};
OS   Candidatus Aminicenantes bacterium RBG_19FT_COMBO_58_17.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797275 {ECO:0000313|EMBL:OGD39592.1, ECO:0000313|Proteomes:UP000178644};
RN   [1] {ECO:0000313|EMBL:OGD39592.1, ECO:0000313|Proteomes:UP000178644}
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:OGD39592.1}.
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DR   EMBL; MEYD01000023; OGD39592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5C9R1; -.
DR   STRING; 1797275.A2V45_12795; -.
DR   Proteomes; UP000178644; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 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   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OGD39592.1}.
FT   DOMAIN          78..571
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   574 AA;  62374 MW;  A68E30E2AE32DAFE CRC64;
     MPHRRLSRPT FVVLVVLAVG GLSGCVKKQP ADLVLTNGKI ITLEEIAPTA EALAVAGDRI
     VAVGTAKKIK PFIGTSTRVI DLQGQTAIPG FIDSHAHFTG VGEARMILDL TRAKNWDEIV
     SIVAEAARNA KPGEWIRGRG WHQEKWDKTP EPNVDGLPFH DALSRMTSEN PVLLEHASGH
     SCLANAKAME LGGITKTTPD PAGGEIVRDA RGNPIGAFRE TAQGLIGRSL YGSELKKTEA
     ERVEEERKAI ALAVQECLSK GITSLHDAGA SFATIDIYRE LAEQGKLGVR IYAMISAGNT
     ELQQSLARYR IIGAGQNHLT VRTIKRFIDG ALGAHGAWLL EPYADLPASA GLNTMPIDTL
     KETARLAIEN GFQLCTHAIG DRGNREILNI YEEAFAAHPE QKDLRWRVEH AQHLAPADIP
     RFGRLGVIAA MQGVHCISDG PWVVKKIGEK RAKEGAYVWR SLMEGGAIIC NGTDAPVEDV
     DPIPSFYATV TRKMKDGTMF FPEQRLSRDE ALRTYTLNGA YAAFQEDLLG SLKPGKLADI
     TVLSKDIMTV AEEEIPATEV RLTIVGGQVL YQKN
//
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