ID A0A1Q8CU56_9PSEU Unreviewed; 461 AA.
AC A0A1Q8CU56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:OLF17895.1};
GN ORFNames=BU204_08780 {ECO:0000313|EMBL:OLF17895.1};
OS Actinophytocola xanthii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF17895.1, ECO:0000313|Proteomes:UP000185596};
RN [1] {ECO:0000313|EMBL:OLF17895.1, ECO:0000313|Proteomes:UP000185596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-183 {ECO:0000313|EMBL:OLF17895.1,
RC ECO:0000313|Proteomes:UP000185596};
RA Wang W., Yuan L.;
RT "The draft genome sequence of Actinophytocola sp. 11-183.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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:OLF17895.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSIE01000013; OLF17895.1; -; Genomic_DNA.
DR RefSeq; WP_075125090.1; NZ_MSIE01000013.1.
DR AlphaFoldDB; A0A1Q8CU56; -.
DR STRING; 1912961.BU204_08780; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000185596; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01314; D-HYD; 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; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
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; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000185596}.
FT DOMAIN 50..436
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 150
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 461 AA; 49666 MW; 56B5D02985B96DAC CRC64;
MRTLIRNGTV VNAGGALAAD VLVDGETIAA VTAPGLFDTA DRVIEAQGRY VLPGGIDAHT
HMEMPFGGTF SADTFATGTA AAAWGGTTTI IDFAVQTKGT SLLSTLDKWH EKADGRCAVD
YGFHMIVSDV NDQSLKEMES CIDAGVNSFK MFMAYPGVFY ATDGEILRAM QKATETGSMI
MMHAENGIAI DELVAQALAS GRTDPVEHGR TRPPELEGEA TSRAIQLARV TGAPLYIVHL
SARHALEAVA AARNTGQNVF AETCPQYLYL SIEDLAKPDF EGSKYVASPP LRPRDHQADL
WRGLRTNDLS VVSTDHCPFC FVDQKELGRG DFSKIPNGMP GVEHRMDLLH QGVVAGELTL
ARWVEVCSAT PARMFGLYGR KGVIAPGADA DIVVYDPVAR QTISARTHHM NVDYSAYEGM
EITGRVETVL SRGSVVVSGG AFHGREGHGR FLSRELSQYL V
//
