ID A0A1H0R198_9RALS Unreviewed; 472 AA.
AC A0A1H0R198;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:SDP23304.1};
GN ORFNames=SAMN04488595_10641 {ECO:0000313|EMBL:SDP23304.1};
OS Ralstonia sp. 25mfcol4.1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1761899 {ECO:0000313|EMBL:SDP23304.1, ECO:0000313|Proteomes:UP000199332};
RN [1] {ECO:0000313|EMBL:SDP23304.1, ECO:0000313|Proteomes:UP000199332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25MFCol4.1 {ECO:0000313|EMBL:SDP23304.1,
RC ECO:0000313|Proteomes:UP000199332};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNJO01000006; SDP23304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0R198; -.
DR STRING; 1761899.SAMN04488595_10641; -.
DR OrthoDB; 5687299at2; -.
DR Proteomes; UP000199332; 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:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 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;
FT DOMAIN 55..447
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 156
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 472 AA; 51443 MW; AEFBB7FC534C8EC5 CRC64;
MPADNHLDLV IRNADVVTAS DRFRCDIGVR GGKIVALGHG LPAAQQEVDA TGLLALPGGV
DGHCHLDQPM PDGMRMADDF FTGTRAAVCG GTTTVIPFAA QEKGASLKAA VADYHCRADG
RAVIDYAFHL IVADPTPAVL QDELPSLIRQ GYSSFKVYMT YDDLKLSDRE MLEVLDVARQ
NQALVMVHAE NADCISWLTD RLTGEGRIAP RFHGLARPAV VEREATHRAI SFAELVDVPI
LIVHVSGKEA IEQIRWAQGR GLKILAETCP QYLYLTAEDM GLPGDDGYEG AKCICSPPPR
DPENQAAVWR ALANGVFSVF SSDHAPFNYD DPEGKKLGGV AQPFDHIPNG VPGIETRLPL
LFDGVQRGKL SLHQFVELTS YRPARIYGLY PRKGTIAVGA DADIVLWDPA RKVRIANSNL
HHAVDYTPYE GIEVTGWPMT TFSRGEMIVR NGEYLEPAAG RGRFLEAGQP EL
//