ID   A0A3D9KB13_9BACL        Unreviewed;       663 AA.
AC   A0A3D9KB13;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Dihydroorotase-like cyclic amidohydrolase {ECO:0000313|EMBL:RED83340.1};
GN   ORFNames=DFP98_108183 {ECO:0000313|EMBL:RED83340.1};
OS   Cohnella phaseoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=456490 {ECO:0000313|EMBL:RED83340.1, ECO:0000313|Proteomes:UP000256977};
RN   [1] {ECO:0000313|EMBL:RED83340.1, ECO:0000313|Proteomes:UP000256977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7287 {ECO:0000313|EMBL:RED83340.1,
RC   ECO:0000313|Proteomes:UP000256977};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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:RED83340.1}.
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DR   EMBL; QRDZ01000008; RED83340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9KB13; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000256977; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR   InterPro; IPR013108; Amidohydro_3.
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:RED83340.1}.
FT   DOMAIN          414..521
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          40..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  72500 MW;  208E49DF7FC7AA9F CRC64;
     MTNSRRKSRN RRIFPIMISV LALFIAGGIW AASALLKDGS DAGPSVSPSA TKGGTASSSS
     TESGNGSASP SASQPAEEAA GEIDTPTSSE LEQTYDIVIE NGRVINPETK LDREGLNVAV
     QDGRIMLVTD QKLKGERVID ATGLVVAPGF IDNLSYDPNP VGVWNKIADG VTANIAMHGG
     TASPEKWYPY YERDKPPVHF GASFFYTQAR NQFKLSRYDT AKPEQTQKLV DQAERALNNG
     VLGISFSLEY VPGVNDKEIL PLMKLAHEYN VPVYFHARYS DMEEPGTNID ALNELIGYAR
     ASGAAVHIDH INSTGGTFSM QQSLKMVEDA IAEGLDITSC IYPYDYWGTY LNSARFDEGW
     QERFRISYED LQIAGTEERL TKETFRKYQK EGKLAVAYAI PKQDVIDSLK APYVMIGSDA
     ILEPGFNNHP RASGTFARTV GLYVREQQVI SLSDAIAKMS LLPAQRLEKQ APALKKKGRI
     AKGMDADIVV FDYDKISDQS TVAKPEIVSA GIEYVLVNGQ VALDQDGINK KIRVGQPIKS
     EFVRVKSGGP ALVWDESKLT LLEYRDSNYV DVEALKEQGY SVQWDKTGRS GSVASGTDSG
     NADVPAPAVG ELILERGHQL AWEDGSRTEL LSVGERNYLP LSALEAHGWQ LTKDGQTYKL
     AKA
//