ID A0A327MBB7_9PROT Unreviewed; 420 AA.
AC A0A327MBB7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:RAI59775.1};
GN ORFNames=DOO78_05825 {ECO:0000313|EMBL:RAI59775.1};
OS Roseicella frigidaeris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseicella.
OX NCBI_TaxID=2230885 {ECO:0000313|EMBL:RAI59775.1, ECO:0000313|Proteomes:UP000249065};
RN [1] {ECO:0000313|Proteomes:UP000249065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB-1506 {ECO:0000313|Proteomes:UP000249065};
RA Khan S.A.;
RL Submitted (JUN-2018) 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:RAI59775.1}.
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DR EMBL; QLIX01000003; RAI59775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327MBB7; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000249065; 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 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 NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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:RAI59775.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249065};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 420 AA; 43720 MW; 929B1DA439AA042B CRC64;
MAADAAVRLA ELVFAALREA SEDPPGVSRA SYGEGERAAH AICRAAAEAI GLEVEADPVG
TLSMTLPGMN RDLPPVVIGS HLDAVPHGGN FDGAAGVVMG LALAARLRRE GRLLPRDLVV
LGIRAEEMCW FPMLYLGSRA AFGLLPPEAP DTLRRTDSGR TLAEHMAEEG FDPDFIRQSR
ASLDPAFIHA FLEPHIEQGP VLVEAGLPAA IVTGIRGSVR FRHGRARGAW AHAGAVPRQG
RRDAVLAVAH LAGALERFWT EAEAEGRDLV LTMGEVSTDP AMHGPTKVPG EVAFTLDIRS
EDAAVLQDVE ALLQEEAAEA AAGRGVALET GPRLYVPPAI MDARLRAALA EGAAAAGVPV
MSMASGAGHD ALTFAGLGVP TAMLFIRNEN GSHNPAEAMA MADFAAALDV LAAAIGPIAA
//
