ID A0A2T8HQI7_9RHOB Unreviewed; 484 AA.
AC A0A2T8HQI7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:PVH27701.1};
GN Name=hydA {ECO:0000313|EMBL:PVH27701.1};
GN ORFNames=DDE20_16475 {ECO:0000313|EMBL:PVH27701.1};
OS Pararhodobacter oceanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=2172121 {ECO:0000313|EMBL:PVH27701.1, ECO:0000313|Proteomes:UP000245911};
RN [1] {ECO:0000313|EMBL:PVH27701.1, ECO:0000313|Proteomes:UP000245911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM505 {ECO:0000313|EMBL:PVH27701.1,
RC ECO:0000313|Proteomes:UP000245911};
RA Wang X.-L., Du Z.-J.;
RT "Pararhodobacter oceanense sp. nov., isolated from marine intertidal
RT sediment.";
RL Submitted (APR-2018) 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:PVH27701.1}.
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DR EMBL; QDKM01000010; PVH27701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HQI7; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000245911; 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:UP000245911}.
FT DOMAIN 47..418
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 147
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 484 AA; 52921 MW; 7D041F456B082780 CRC64;
MSTIIKNGTI VTADLTYEAD VRVEDGVITE IGKNLKGGTE LDASGCYVMP GGIDPHTHLE
MPFMGTYSTD DFDSGTRAAL AGGTTMVVDF ALPNQGESLL DALKRWDNKS TRANCDYSFH
MAVTWWGEQV FDDMEAVVRE RGINTFKHFM AYKGALMVND DEMYSSFKRL SELGATAMVH
AENGDVVAEL TAKLLAEGNT GPEAHAYSRP PQVEGEATNR AIMIADMAGV PLYVVHTSCE
ESHEAIRRAK QAGKRVWGEP LIQHLTLDES EYFNADWDHA ARRVMSPPFR NKKHQDSLWA
GLQSGSLSVV ATDHCAFTTE QKRYGVGDFS KIPNGTGGLE DRMPMLWTHG VATGRLTPNE
FVAVTSTNIA KILNCYPKKG AVLVGADADL VVWDPEKEKT ISAGNQQSAI DYNVFEGKHV
KGLPRFTLTR GHVAVHDGEM RHQPGHGKFV ARAPNATVNK ALSQWKDITA PRPVQRSGIP
ATGV
//
