ID A0A136KXU1_9CHLR Unreviewed; 491 AA.
AC A0A136KXU1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-hydantoinase {ECO:0000313|EMBL:KXK14133.1};
DE EC=3.5.2.2 {ECO:0000313|EMBL:KXK14133.1};
GN ORFNames=UZ15_CFX003003113 {ECO:0000313|EMBL:KXK14133.1};
OS Chloroflexi bacterium OLB15.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK14133.1, ECO:0000313|Proteomes:UP000070332};
RN [1] {ECO:0000313|EMBL:KXK14133.1, ECO:0000313|Proteomes:UP000070332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB15 {ECO:0000313|EMBL:KXK14133.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK14133.1}.
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DR EMBL; LMZS01000168; KXK14133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KXU1; -.
DR STRING; 1617416.UZ15_CFX003003113; -.
DR PATRIC; fig|1617416.3.peg.3285; -.
DR Proteomes; UP000070332; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:KXK14133.1}.
FT DOMAIN 49..464
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 148
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 491 AA; 53811 MW; 24220AEBADD4AD77 CRC64;
MGTLFKNGTV ITAGEQSRAD VLVEGEVVSL IGRDLDPAGH TVIDCTGKYL LPGGIDVHTH
LDLPFGGTFS NDDFDVGHKA AAFGGTTAHI DFVIQPKGGT LHDGLATWRK KAQPAQIDYA
FHMAVTDLRD DVMDEIPSMV DEGITSLKLF MAYKNVFQVD DKTLFKTMQV AAKHGQIVMV
HAENGDVENT LTPELLAAGK TDPVYHAASR PPEIEGEATN RAVVMSGLSG CPLYVVHMTC
EPSIDALRRG RALGYPVMGE TCVQYFFLTV EEHMAQPDFH GSKYVCSPPI RSKHDQQVLW
RAVKDGTLQV VSTDHCDFWF DGGKGPWQEW AAAHNGGDWV EYERQDPSYR RPGKELGRGN
FAKIPNGLPA IEDRLMMVWD GGVNTGILSP SRFVELNCTN PAKIFGMYPK KGTIAVGSDA
DIVVWDPNAK HTLSAATQHM RCDYNLFEGH TVTGKPVMVF QRGNKLVDGD QWFGKNGQGQ
FIHREAGAPV L
//
