ID A0A1J0WJX9_9RHOB Unreviewed; 416 AA.
AC A0A1J0WJX9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:APE44641.1};
GN ORFNames=BOO69_15405 {ECO:0000313|EMBL:APE44641.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE44641.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE44641.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE44641.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-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}.
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DR EMBL; CP018076; APE44641.1; -; Genomic_DNA.
DR RefSeq; WP_071972989.1; NZ_CP018076.1.
DR AlphaFoldDB; A0A1J0WJX9; -.
DR STRING; 1917485.BOO69_15405; -.
DR KEGG; suam:BOO69_15405; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000181897; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:APE44641.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..309
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 416 AA; 45162 MW; F66A82D577553C76 CRC64;
MPAPGENLKI NPDRLWDSLM EMAKIGPGVA GGNNRQTLTD EDAEGRALFR KWCEDAGCTM
GLDQMGNMFA RREGTDPDAL PVYVGSHLDT QPTGGKYDGV LGVLAGLEIV RTLNDLGVKT
KHPIVVTNFT NEEGTRYAPA MLSSGVFAGI HTQDWAYARV DAQGKSFGDE LKRIGWRGEE
ETGARKMHAF FELHIEQGPI LEAEEKQIGV VTHGQGLSWT QVTVTGKDSH TGSTPMPMRR
NAGLGMARIL EKVDEIAWSH KPHAVGAAGH IDVYPNSRNV IPGKVVFTVD FRSPDLSVIE
DMEKRLREEG QKIADDMELG IEFEKVGGFD PVAFDEDCVS AVRDAAERLG YSHMNLISGA
GHDACWINRV APTAMVMCPC VDGLSHNEAE EISKEWAQAG TDVLLHAVVE TAGVAG
//
