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Database: UniProt
Entry: K1MBT8_9LACT
LinkDB: K1MBT8_9LACT
Original site: K1MBT8_9LACT 
ID   K1MBT8_9LACT            Unreviewed;       411 AA.
AC   K1MBT8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=HMPREF9706_01572 {ECO:0000313|EMBL:EKB53494.1};
OS   Facklamia hominis CCUG 36813.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB53494.1, ECO:0000313|Proteomes:UP000004465};
RN   [1] {ECO:0000313|EMBL:EKB53494.1, ECO:0000313|Proteomes:UP000004465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB53494.1,
RC   ECO:0000313|Proteomes:UP000004465};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL   Submitted (JUL-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:EKB53494.1}.
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DR   EMBL; AGZD01000012; EKB53494.1; -; Genomic_DNA.
DR   RefSeq; WP_006908880.1; NZ_JH932292.1.
DR   AlphaFoldDB; K1MBT8; -.
DR   STRING; 883111.HMPREF9706_01572; -.
DR   PATRIC; fig|883111.3.peg.1592; -.
DR   HOGENOM; CLU_031758_0_1_9; -.
DR   OrthoDB; 9815027at2; -.
DR   Proteomes; UP000004465; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01293; Bact_CD; 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   PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR   PANTHER; PTHR32027:SF0; CYTOSINE DEAMINASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000004465}.
FT   DOMAIN          38..398
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   411 AA;  46538 MW;  FDA2B85001F4396E CRC64;
     MLIKNVFIEN QEKPSDIRIL DGVITEIADQ IEATDQEEVI DATGKLALPP FIEPHVHLDS
     VLTAGQPKWN ESGTLFEGIE TWSLRKQSLT YEDVKDRAGR AIRKQAANGI QFVRTHVDTT
     DPKLTALRAL IDLREEVKDF MEIQIVAFPQ EGILSFKNGY ELLEEALKLG ADVVGAIPHY
     EFTREYSVTS LEMMMELAQK YQVLVDVHCD EIDDEASRGL EVLATLALET GMKGRVTASH
     TTAMHSYNNA YVAKLMRLLR LSEINFIANP LVNTHLQGRV DNYPKRRGMT RVKELLANGN
     NVAFGHDDLF DPWYPLGDGN MLEVIHMGLH IGHMMGYQEI MDSYRFVTHN AARCLNISDR
     YGIEVGKPAN LIIMNQSNFY HVLNERSEVL YNIHEGKVIA KTQPKVKEVL F
//
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