ID A0A146GAN3_TERSA Unreviewed; 457 AA.
AC A0A146GAN3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:GAT33636.1};
GN ORFNames=TSACC_22053 {ECO:0000313|EMBL:GAT33636.1};
OS Terrimicrobium sacchariphilum.
OC Bacteria; Verrucomicrobiota; Terrimicrobiia; Terrimicrobiales;
OC Terrimicrobiaceae; Terrimicrobium.
OX NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT33636.1, ECO:0000313|Proteomes:UP000076023};
RN [1] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Terrimicrobium sacchariphilum NM-5(T), a
RT facultative anaerobic soil bacterium of the class Spartobacteria.";
RL Genome Announc. 0:0-0(2017).
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:GAT33636.1}.
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DR EMBL; BDCO01000002; GAT33636.1; -; Genomic_DNA.
DR RefSeq; WP_075079348.1; NZ_BDCO01000002.1.
DR AlphaFoldDB; A0A146GAN3; -.
DR STRING; 690879.TSACC_22053; -.
DR InParanoid; A0A146GAN3; -.
DR OrthoDB; 9765462at2; -.
DR Proteomes; UP000076023; 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; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
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 457 AA; 49827 MW; 385249494A5A9B02 CRC64;
MALLIKNGEI VTADSRYVAD IWCEGETITH IAPDIEVPAG AEVIDASGKY VFPGFIDPHT
HIYLPFMGTY SKDDYESGTK AALIGGTTTI FDMCTPGRGT TPLEGFETWT RQASGKAACD
YAFHVGVAGF DESTPAQLRE IVAKGIGSFK IFLAYKGALG IDDEELYETL RIAKELGVIT
AAHCENSTLI SSLQKDLLAR GVTGTEGHHA SRPPRVEAEG VHHLMTFAEL TGASVYIVHL
SCVEALEEAL RARLRGVDVS IETLIQYLLI DKNYAELGNF EGAKYVMSPP LRDASNQPIL
WNALRQGLIQ TVATDHAPFD FFTQKRMGEH DFTKIPNGIP AIEDRVNLLY THGVAEGRLD
LQTFVAVAST NAAKTFNLFP RKGTIQPGCD ADLVVYDPAY RGTISAATQT QNVDYNAFEG
WEIKGKPTHV SVRGQLAVRD GKFVGTPGRG RLLRTTR
//
