ID A0A1H9SP69_9ACTN Unreviewed; 434 AA.
AC A0A1H9SP69;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Allantoate deiminase {ECO:0000313|EMBL:SER86119.1};
GN ORFNames=SAMN05443377_11425 {ECO:0000313|EMBL:SER86119.1};
OS Propionibacterium cyclohexanicum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=64702 {ECO:0000313|EMBL:SER86119.1, ECO:0000313|Proteomes:UP000198815};
RN [1] {ECO:0000313|EMBL:SER86119.1, ECO:0000313|Proteomes:UP000198815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16859 {ECO:0000313|EMBL:SER86119.1,
RC ECO:0000313|Proteomes:UP000198815};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOGZ01000014; SER86119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9SP69; -.
DR STRING; 64702.SAMN05443377_11425; -.
DR Proteomes; UP000198815; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198815};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 227..324
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 231
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 289
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 302
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 434 AA; 46586 MW; 51016A355EDED62C CRC64;
MSAHSTTGTM SEMSAVRRDD QARLIMARCD ELASHSSMDG GIERVYLSPE HAQVDALAAQ
WMAEAGLATW RDASGSRVGR LEGDRPGLPA LILGSHLDTV PDAGRYDGIL GVLLEIEVAR
RIGASGARLP FALETYAFHE EEGVRFGATL LCSRALAGTW NDDLWQLHDA QGVSLRQAFS
DFGLCPERIG EAAKKPAEVI GYLEAHIEQG PALEAAGLPL GVVTSIAGAR RFEITITGEA
RHAGGTPYPR RRDALVGAAE AVAAVERIGQ QQDVIATVGQ LRVEPGAVNI VPGEAVFSLD
LRAETDEARD RAWDLIHEEF EAICRRRGLT LDINQIHQAH GVGCAPALMD AIGAGITQAT
AATEPPMRMW SRAGHDAMAV ADLCEVAMLF VRCHDGISHA PDESVLTEDV AVALDAYEAA
IWQVAEHYRR RQGA
//
