ID A0A1V2H087_9PROT Unreviewed; 418 AA.
AC A0A1V2H087;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:ONG50461.1};
GN ORFNames=BKE38_18230 {ECO:0000313|EMBL:ONG50461.1};
OS Pseudoroseomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG50461.1, ECO:0000313|Proteomes:UP000188879};
RN [1] {ECO:0000313|EMBL:ONG50461.1, ECO:0000313|Proteomes:UP000188879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|EMBL:ONG50461.1,
RC ECO:0000313|Proteomes:UP000188879};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Roseomonas sp. strain M3.";
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 -!- 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:ONG50461.1}.
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DR EMBL; MLCO01000188; ONG50461.1; -; Genomic_DNA.
DR RefSeq; WP_076958744.1; NZ_MLCO01000188.1.
DR AlphaFoldDB; A0A1V2H087; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000188879; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ONG50461.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188879};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 220..304
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
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 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 418 AA; 44902 MW; 7DE59830F0488C38 CRC64;
MSESVAPNLI AAVDEARQWD RLMQMAKLGA IPGDGVNRPC LSPLDREARR LLIGWAEALG
LAVATDELGN LFLRHEGSDP EAAPVLTGSH MDSQPNGGRF DGIWGVLAGL EAVQAIREAG
LATRRPIEVV AWTNEEGGRY APGCMGSMAW SGFAKPDSWD AVVDPDGIPF RAALDEHLAA
EADLPRRPLG AYRPHAYVEA HIEQGPRLES GGLDIGVVTG IQGSRWFLVE IEGKTDHAGT
TPLSQRQDAV QDMVRAITAL NRLMQDPADV LRFTVGKVEV FPNSSNTVAD RARFTIDFRH
PDKDVLLARG AAIPGVIQAA LTSCRATVTE RFFALPVEFQ PEVPGAVERA ALAQGLKPLR
MPSGAFHDAQ FLVPLCPSGM IFVPCRDGVS HHPSEYSTPE QLAKGTRVLA AALLELAA
//
