ID R6J688_9FIRM Unreviewed; 410 AA.
AC R6J688;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:CDB45827.1};
GN ORFNames=BN533_00952 {ECO:0000313|EMBL:CDB45827.1};
OS Phascolarctobacterium faecium.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Phascolarctobacterium.
OX NCBI_TaxID=33025 {ECO:0000313|EMBL:CDB45827.1, ECO:0000313|Proteomes:UP000014944};
RN [1] {ECO:0000313|EMBL:CDB45827.1, ECO:0000313|Proteomes:UP000014944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:207 {ECO:0000313|Proteomes:UP000014944};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDB45827.1}.
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DR EMBL; CBDS010000057; CDB45827.1; -; Genomic_DNA.
DR AlphaFoldDB; R6J688; -.
DR STRING; 1262914.BN533_00952; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_9; -.
DR Proteomes; UP000014944; 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:CDB45827.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014944};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 214..313
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 214
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 275
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 288
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 410 AA; 43707 MW; 0EEC2ACA1FE7B08E CRC64;
MQAINKERVA GLLQGLAQFG KTEHGITRLA YTAEDKAAQE WLLKQIQDLQ LKLSVDAVGN
VFLRREGKNT DLAPVAMGSH IDTVVQGGAY DGTVGVVGAL EVLYMLQDEE LERPIEVIIF
RAEESSRFGF ATIGSKLMAG VGDPDKFSGA AKEGAVTFKE ALTEWGCDPA AYKQARKAAG
CFKSFWEIHI EQGKVLEETG ERIGIVHNIA APTRFKIIVE GIADHSGATP MGFRKDALVS
AARLVIAIEE AATNEAESGT VATVGVLDVE PSSINVVPGK ATLWVDLRGV DEESINCALS
DIRDAVSEIA KNDSITITMD MLTADNPVAL SEELAAKLDV ICAAKGIAYR HMNSGAGHDA
MHMAKLAPAS MLFVPCKGGI SHNPAEYADN EDICLAIEIL AEAVKEEASA
//
