ID A0A1I4QQ56_9PSEU Unreviewed; 466 AA.
AC A0A1I4QQ56;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:SFM41846.1};
GN ORFNames=SAMN05421805_101205 {ECO:0000313|EMBL:SFM41846.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM41846.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM41846.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM41846.1,
RC ECO:0000313|Proteomes:UP000199398};
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; FOUP01000001; SFM41846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4QQ56; -.
DR STRING; 455193.SAMN05421805_101205; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000199398; 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..440
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 155
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 466 AA; 50559 MW; EC480C1C02AB0C3F CRC64;
MNRTIIRGGL VITATEELRA DVLVDGERIA AIAAPEVAEQ WVPAADTVID AGGHYVIPGG
VDGHTHMQMP FGGTFASDTF ETGTRAAAWG GTTTIVDFAI QPVGGSLREG LDAWHAKADG
QCAIDYGFHM ILSDVGDEAL KEMDALVAEG ITSFKLFMAY PGVFYSDDGQ ILRAMQQAAD
NGALTMMHAE NGIAIDVLVR QALAAGRTDP GYHGQVRHPL LEAEATHRAI QLSRVAGAPL
YVVHVSAAEA VAELTRARDD GLNVFGETCP QYLFLSLDDL ARPEFEGAKF VCSTPLRPAE
HQADLWRALR TNDLSVVSTD HCPFCFKDQK ELGRGDFSKI PNGIPGVENR VDLLHQAVVE
GHISRRRWVE LACTTPARMF GLHPRKGTIA PGADADIVIY DPHREQVLSA QTHHMNVDYN
AYEGKPVTGA VRTVLSRGRV IVDDGEYLGE AGHGRFLRRD TCQYLV
//