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Database: UniProt
Entry: B5ZYK4_RHILW
LinkDB: B5ZYK4_RHILW
Original site: B5ZYK4_RHILW 
ID   B5ZYK4_RHILW            Unreviewed;       426 AA.
AC   B5ZYK4;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:ACI57621.1};
DE            EC=3.5.1.87 {ECO:0000313|EMBL:ACI57621.1};
GN   OrderedLocusNames=Rleg2_4363 {ECO:0000313|EMBL:ACI57621.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI57621.1, ECO:0000313|Proteomes:UP000008330};
RN   [1] {ECO:0000313|EMBL:ACI57621.1, ECO:0000313|Proteomes:UP000008330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304 {ECO:0000313|EMBL:ACI57621.1,
RC   ECO:0000313|Proteomes:UP000008330};
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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}.
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DR   EMBL; CP001191; ACI57621.1; -; Genomic_DNA.
DR   RefSeq; WP_012559723.1; NC_011369.1.
DR   AlphaFoldDB; B5ZYK4; -.
DR   STRING; 395492.Rleg2_4363; -.
DR   KEGG; rlt:Rleg2_4363; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_024588_6_1_5; -.
DR   Proteomes; UP000008330; Chromosome.
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   GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACI57621.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          210..313
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         215
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         278
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         291
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   426 AA;  45487 MW;  BFE031286FF49C25 CRC64;
     MSRNLPVNAG RIAGDIEALA AITEPGHPWT RRAFSPLFLE GRAYIEARMK AAELETRIDA
     TGNLIGRRTG RKPWLGTIMV GSHSETVPDG GRFDGIAGVI SALEVARALS DQAIELDHDL
     EIVDFLAEEV SIFGVSCIGS RGMTGQLPEA WLSRISDGRD LAEGIAEVGG EPGVLAQQKR
     PDLAGFLELH IEQGPVLEAE REDIGIVTAI AGITRIEITV EGRADHAGTT PMDRRADALV
     AAAQLVLDIR NAAAELAKTP GHFAATVGEF RIEPNAANVV PSKVVLLIDG RAEIRADMEA
     FCRWLDGHVE KLATAYGVTI RTPNRVSDNM PTPGDAGLLS TLEAACERVG AKHRRMASGA
     GHDTAWIAKV APAAMIFVPC REGRSHSGDE WAENDDIALG AAVLFEAVRE MDKDLTREKA
     DGTHTG
//
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