ID S0JEZ3_9ENTE Unreviewed; 409 AA.
AC S0JEZ3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:EOT26328.1};
GN ORFNames=OMQ_02103 {ECO:0000313|EMBL:EOT26328.1};
OS Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT26328.1, ECO:0000313|Proteomes:UP000014136};
RN [1] {ECO:0000313|EMBL:EOT26328.1, ECO:0000313|Proteomes:UP000014136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT26328.1,
RC ECO:0000313|Proteomes:UP000014136};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 (Illumina
RT only assembly).";
RL Submitted (MAR-2013) 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:EOT26328.1}.
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DR EMBL; AHYT01000010; EOT26328.1; -; Genomic_DNA.
DR RefSeq; WP_016175864.1; NZ_KE136523.1.
DR AlphaFoldDB; S0JEZ3; -.
DR STRING; 41997.RV16_GL001978; -.
DR MEROPS; M20.976; -.
DR PATRIC; fig|1139996.3.peg.2068; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_9; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000014136; Unassembled WGS sequence.
DR GO; GO:0047652; F:allantoate deiminase activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0009442; P:allantoin assimilation pathway; IEA:InterPro.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017591; Allantoate_amidohydrolase.
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; TIGR03176; AllC; 1.
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:EOT26328.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014136};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 210..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 125
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 273
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 286
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 409 AA; 45359 MW; 4802AC51616BDBDC CRC64;
MDLNKVLADN IKNLSQIGSD PTGGMTRLLY TDSWLEAQKY VANQLTDAGL TATFDEVGNL
FGRIEGTKYP EETILSGSHI DTVVNGGTLD GQFGVIAAYV AIQYLLATYG QPLRSLEVIS
MAEEEGSRFP TVFWGSKNFV REAKRSDVED IADFEGKKFV DEMRRQGFDF RDESVPKRDD
IRAFVEIHIE QGNVLENEAL QIGVVNNIAG QRRYTIVLKG EANHAGTTPM GYRKDAVYGF
SKICSEIIDR AVQVGDPLVV TFGKVEPKPN TVNVVPGEVL FTMDCRHTDQ EVLKNFTEEA
EAFMKEVAKD HQLDIAIDLW MDEAPVPMND DIVATVEKAA KAEKMKYKMM HSGAGHDSQI
IAPHYPSAMI FVPSTKGISH NPAEETKHED LVAGVKVLAK ALYELAYKE
//
