ID T0D9L3_ALIAG Unreviewed; 409 AA.
AC T0D9L3; A0A9E6ZF03;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:UNO48687.1};
GN ORFNames=K1I37_18835 {ECO:0000313|EMBL:UNO48687.1};
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:UNO48687.1, ECO:0000313|Proteomes:UP000829401};
RN [1] {ECO:0000313|Proteomes:UP000829401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3922 {ECO:0000313|Proteomes:UP000829401};
RX PubMed=36240455; DOI=10.1093/g3journal/jkac225;
RA Leonardo I.C., Barreto Crespo M.T., Gaspar F.B.;
RT "Unveiling the complete genome sequence of Alicyclobacillus acidoterrestris
RT DSM 3922T, a taint-producing strain.";
RL G3 (Bethesda) 12:0-0(2022).
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; CP080467; UNO48687.1; -; Genomic_DNA.
DR RefSeq; WP_021295978.1; NZ_AURB01000113.1.
DR STRING; 1356854.N007_04695; -.
DR KEGG; aaco:K1I37_18835; -.
DR Proteomes; UP000829401; Chromosome.
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:UNO48687.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000829401};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 208..306
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="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 125
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 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; 43489 MW; 8203F4C2A62A89F1 CRC64;
MVNQERLWRR LMALGEVGKQ ASGGITRLAF TREEREAKDL VSKWMQEAGL EVREDAVGNL
IGRKEGVHPE AAVVLAGSHI DSVFHGGNFD GPLGVLAAVE ALQCMGEAGI QPERPIEVVA
FTDEEGARFR FGMTGSRGLA GNLRIEELEA QDDAGVSIAE AMRACGFNPA RIGEAARPKG
SVHAYVEVHI EQGKVLEQTG LQVGVVTGLA GPLWLKFTVT GTAGHAGTTP MALRSDALTG
AAEIILEIEQ AAARETRTVG TVGQLTVYPG GVNIIPGRVE FTLDLRDVDA STRRAVADEI
CRNAEQICAN RGLTLSVETL QDIAPLACAK EIQDAIYDAC ETVGIKTMPV VSGAGHDCMQ
LQDLCPVGMI FVRSKDGISH HPDEWSAPED CAAGASVLYH TLLKLAHLG
//
