ID N1ZP31_9CLOT Unreviewed; 422 AA.
AC N1ZP31;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Hydantoinase/carbamoylase family amidase {ECO:0000313|EMBL:EMZ15798.1};
DE SubName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:USF30957.1};
DE EC=3.5.1.87 {ECO:0000313|EMBL:USF30957.1};
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:NDO45398.1};
GN Name=hyuC {ECO:0000313|EMBL:USF30957.1};
GN ORFNames=C820_00161 {ECO:0000313|EMBL:EMZ15798.1}, C820_002401
GN {ECO:0000313|EMBL:USF30957.1}, FMM67_00845
GN {ECO:0000313|EMBL:NDO45398.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ15798.1};
RN [1] {ECO:0000313|EMBL:EMZ15798.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ15798.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:NDO45398.1, ECO:0000313|Proteomes:UP000462571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|Proteomes:UP000462571}, and MD294
RC {ECO:0000313|EMBL:NDO45398.1};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF30957.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF30957.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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}.
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DR EMBL; AQFQ01000003; EMZ15798.1; -; Genomic_DNA.
DR EMBL; VIRC01000004; NDO45398.1; -; Genomic_DNA.
DR EMBL; CP097810; USF30957.1; -; Genomic_DNA.
DR RefSeq; WP_004033455.1; NZ_VIRC01000004.1.
DR AlphaFoldDB; N1ZP31; -.
DR STRING; 97138.C820_00161; -.
DR PATRIC; fig|97138.3.peg.163; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_2_1_9; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000012445; Chromosome.
DR Proteomes; UP000462571; 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:NDO45398.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012445};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 225..318
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 422 AA; 47267 MW; 18846900E8807D77 CRC64;
MYKCDVKRME DKIKTFSQFG DAGHGGITRY SLSEEAIQAR DEFVKRMTAI GASIETDDLA
NIYATIAGSD PNAKRIVMGS HCDSVKNGGN YDGILGVMGA MEVLETVVKE NIPHVHPLTA
MIFTNEEGSE FPPCMMCSGI LAHDYMPERF KDNFEYNKMM ASKSILDPEM TFGKKLENFK
YKGDISNRMS PDKYKALFEL HIEQGPILED ANKNIGVVTC VLGQMIYRVK FYGFAAHAGT
FPMKKRHDAF HAAAEALCYL HEEIDKLGYE DLVYTTGEVV IHPCVNTVIP DFFDFSIDVR
HENPDVLNKV REILATLPKR EWKGCKCEVV LGWNRDTVYW NKELVGYVRE AVEELGISHM
DINSGAGHDA QYISYMLPTT MIFVPSDKGL SHCEVEHTSA QQCTDGASVM LNAVLKADKA
TD
//