ID W4Q2E8_9BACI Unreviewed; 413 AA.
AC W4Q2E8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Amidase {ECO:0000313|EMBL:GAE25524.1};
GN ORFNames=JCM9140_1524 {ECO:0000313|EMBL:GAE25524.1};
OS Halalkalibacter wakoensis JCM 9140.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE25524.1, ECO:0000313|Proteomes:UP000018890};
RN [1] {ECO:0000313|EMBL:GAE25524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE25524.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
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:GAE25524.1}.
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DR EMBL; BAUT01000011; GAE25524.1; -; Genomic_DNA.
DR RefSeq; WP_052002113.1; NZ_BAZN01000011.1.
DR AlphaFoldDB; W4Q2E8; -.
DR STRING; 1236970.JCM9140_1524; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000018890; 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:UP000018890};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 216..312
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 130
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 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 413 AA; 44984 MW; 6A8E2DB1B0A2EC54 CRC64;
MKQLYRVNSQ RMQNRISELA EIGKQTRGGV TRKALTEEDR KAQLLVTKWM EEAGMTVKQD
HFGNIIGRIA GTNPATPAVV IGSHIDTVPN GGNFDGTIGV IGGIEVAQII SEESITINHP
LEVIAFLDEE GTRFDGGLFG SRGMVGKLTE ADLLKKDGQG ISRLEAMQEF GLDPSLMMES
VRKREDMKVF LELHIEQGPY LQAINQPVGI VKGIAGPAWL SVTVKGESGH AGTVPMKLRK
DPMAGAAEMI SEIERICSRQ DDAPTVGTIG KINALPGGTN VIPEQVEFSL DIRDIDLTRR
DACMKEIKEK IELICHKRGL TFHICEHLVQ EPIACAGHVI DTMKHASKLL SVEAPIMISG
AGHDAMMVAD LTDIGLIFVR CKDGISHNPN EWADIDDISI GVSLLFETTL AYC
//