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Database: UniProt
Entry: D1Y4Q0_9BACT
LinkDB: D1Y4Q0_9BACT
Original site: D1Y4Q0_9BACT 
ID   D1Y4Q0_9BACT            Unreviewed;       408 AA.
AC   D1Y4Q0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:EFB90742.1};
DE            EC=3.5.-.- {ECO:0000313|EMBL:EFB90742.1};
GN   ORFNames=HMPREF7215_1063 {ECO:0000313|EMBL:EFB90742.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB90742.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB90742.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB90742.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC       1};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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:EFB90742.1}.
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DR   EMBL; ADFP01000066; EFB90742.1; -; Genomic_DNA.
DR   RefSeq; WP_009164831.1; NZ_ADFP01000066.1.
DR   AlphaFoldDB; D1Y4Q0; -.
DR   STRING; 352165.HMPREF7215_1063; -.
DR   eggNOG; COG0624; Bacteria.
DR   OrthoDB; 9808195at2; -.
DR   Proteomes; UP000006462; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EFB90742.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          213..309
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         213
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         274
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         287
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   408 AA;  44453 MW;  DA89F2F9C86B964C CRC64;
     MSGFERVREL VEAVSQTGRG ERGVSRLALT EADRQAREIV TEEMKSLGMS VTTDACCNLW
     GRFEGGTDRP GVLIGSHLDS VPEGGRYDGV LGVACGLGAA RDILAEDPRP RRSLSVVVFT
     AEESSRFSLA TVGSKAVTGN LSLLDTLRFK DKRGVTLLDA LRAFGGRPER IPRDCLAPAS
     YHSYFELHIE QGPVLDWNGE DVGIVEAIAA PTRFRLEVIG EQAHSGACPM NLRRDAMAAA
     AEIILAVERA GRTESEFGTV ATVGVCECEP GAMNVVPGRV VLKVDVRGIV EKSIRRACDD
     VMACVERIGE ERGVKVNFTL YSADKPVVMD GLLARRIENV CRARRIKYRR MPSGAGHDAM
     YMAALIPSAL IFVPCKDGIS HNPAEEVDWR RVRPGYEALV ETVRDIVR
//
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