ID A0A401UKX4_9CLOT Unreviewed; 436 AA.
AC A0A401UKX4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:GCD10201.1};
GN ORFNames=Ctaglu_18240 {ECO:0000313|EMBL:GCD10201.1};
OS Clostridium tagluense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=360422 {ECO:0000313|EMBL:GCD10201.1, ECO:0000313|Proteomes:UP000287872};
RN [1] {ECO:0000313|EMBL:GCD10201.1, ECO:0000313|Proteomes:UP000287872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A121 {ECO:0000313|EMBL:GCD10201.1,
RC ECO:0000313|Proteomes:UP000287872};
RA Murakami T., Segawa T., Shcherbakova V.A., Mori H., Yoshimura Y.;
RT "Genome sequencing and assembly of Clostridium tagluense strain A121.";
RL Submitted (NOV-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:GCD10201.1}.
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DR EMBL; BHYK01000008; GCD10201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UKX4; -.
DR OrthoDB; 9765462at2; -.
DR Proteomes; UP000287872; 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; 1.
DR InterPro; IPR006680; Amidohydro-rel.
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; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000287872}.
FT DOMAIN 50..416
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 436 AA; 49671 MW; D4B3099EB737329A CRC64;
MFDLGIVNGR IYIDGRWYEG NLYIKDNKIS TISNEVLEAK EEYDAKGRDI LPGFIDPHVH
FQLTVGTRTS ADDFYKGSRA AAFGGITTYI DFLDPVKNNT SLKKAFNLRR TLAADSVIDY
AFHATIADLD EKPISFINEV KALGIPTIKL FTTYSSSDRR TKDRTIDRLL SHTKETRTLL
LAHSENDGLI LEGGKIPVIQ HERSRPAIAE ISEVIKLAEM TKYRDGRMYI VHTNCGTTVE
RLKENYRSIL NRDFILESCP HYFVFSSSKY LQRDGYLYTM TPPLRSDREV KKLNDQIDNI
FTIGTDHCPF NSTEKNREFI DEMPMGIGGV EYSFPLMYAK FGEKVIDKFT KNPAIVHGLY
PKKGTLLPGS DADIVIFDHN EQYIIKENHS NVDYNLYKDM EITGKVCSTI SKGKFVVKDG
VFIGGKGEYL SRELKY
//