ID A0A1Q2D764_9ENTE Unreviewed; 413 AA.
AC A0A1Q2D764;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:AQP54143.1};
GN ORFNames=BW732_07870 {ECO:0000313|EMBL:AQP54143.1}, CBF34_06290
GN {ECO:0000313|EMBL:RSU02142.1};
OS Vagococcus penaei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=633807 {ECO:0000313|EMBL:AQP54143.1, ECO:0000313|Proteomes:UP000188246};
RN [1] {ECO:0000313|EMBL:AQP54143.1, ECO:0000313|Proteomes:UP000188246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP54143.1,
RC ECO:0000313|Proteomes:UP000188246};
RX PubMed=19897618; DOI=10.1099/ijs.0.012872-0;
RA Jaffres E., Prevost H., Rossero A., Joffraud J.J., Dousset X.;
RT "Vagococcus penaei sp. nov., isolated from spoilage microbiota of cooked
RT shrimp (Penaeus vannamei).";
RL Int. J. Syst. Evol. Microbiol. 60:2159-2164(2010).
RN [2] {ECO:0000313|EMBL:AQP54143.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP54143.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RSU02142.1, ECO:0000313|Proteomes:UP000286995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24833 {ECO:0000313|EMBL:RSU02142.1,
RC ECO:0000313|Proteomes:UP000286995};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019609; AQP54143.1; -; Genomic_DNA.
DR EMBL; NGJV01000010; RSU02142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2D764; -.
DR STRING; 633807.BW732_07870; -.
DR KEGG; vpi:BW732_07870; -.
DR Proteomes; UP000188246; Chromosome.
DR Proteomes; UP000286995; 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:AQP54143.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188246};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 214..311
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 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 217
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 277
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 290
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 413 AA; 45692 MW; BAC903CFD6CB48CD CRC64;
MKHMTDLQQK VEQEVTWLSS IGLDSKGGTT RLLYDDNWVK AQHDLKQKFT TLGLSSHFDQ
VGNLYGRLEG SKYPNETILT GSHVDTVVNG GALDGQFGIV AGYLAINYLK ETYGTPLRTL
EVVSMAEEEG SRFPFAFWGS KNIFGLVNPN DLKYAKDADG IQFSEAMEQA GFSFPTESQQ
AREDIKAFVE IHIEQGNVLE KKEKQVAVVN NIVGQKRYDI TLIGQSNHAG TTPMGYRQDT
VYAMSKMISD SMDRAKELGD PLVLTVGHIA VTPNTVNVVP GKTFFTVDCR HTDGQVLEDF
TNDMMSRFKA IATECDVQIE IDNWMNEAPV PMSEEIVSVL EQACQESNLN YLTMHSGAGH
DSQIFAQHVP TAMLFVPSIN GVSHNPAEAT KIEDLTEGVK ALIASLYKLA YED
//
