ID A0A1D8UWF6_9PROT Unreviewed; 416 AA.
AC A0A1D8UWF6;
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:AOX17926.1};
GN Name=amaB {ECO:0000313|EMBL:GEL64381.1};
GN ORFNames=A0U89_13235 {ECO:0000313|EMBL:AOX17926.1}, KBA01_16670
GN {ECO:0000313|EMBL:GEL64381.1};
OS Kozakia baliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Kozakia.
OX NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX17926.1, ECO:0000313|Proteomes:UP000179145};
RN [1] {ECO:0000313|EMBL:AOX17926.1, ECO:0000313|Proteomes:UP000179145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX17926.1,
RC ECO:0000313|Proteomes:UP000179145};
RX PubMed=27716345;
RA Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL Microb. Cell Fact. 15:170-170(2016).
RN [2] {ECO:0000313|EMBL:AOX17926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX17926.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL64381.1, ECO:0000313|Proteomes:UP000321177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL64381.1,
RC ECO:0000313|Proteomes:UP000321177};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL Submitted (JUL-2019) 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; CP014674; AOX17926.1; -; Genomic_DNA.
DR EMBL; BJVW01000005; GEL64381.1; -; Genomic_DNA.
DR RefSeq; WP_070403442.1; NZ_CP014674.1.
DR AlphaFoldDB; A0A1D8UWF6; -.
DR STRING; 153496.A0U89_13235; -.
DR KEGG; kba:A0U89_13235; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000179145; Chromosome.
DR Proteomes; UP000321177; 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:AOX17926.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179145};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 220..314
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 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 220
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 279
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 292
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
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 416 AA; 44510 MW; 9144CA7CC4083475 CRC64;
MNAAIDNSIG GARAKARCDE LGTTPYSDRP DCLFRPFLGP GHRATLDRIA TWMREAGMGV
AIDEAGNLIG RYEGAKPEAP ALLFGSHVDS VKDGGRYDGM LGVLLGIEAI AAFHQKGKTF
PFALEVIGFG DEEGSRFPTY MMGSRAAAGC LQEIDDAVAD EEGITLCDAL ADWGLNAAHF
ARAKRSNVLA YVEAHIEQAP HLERAGLPLG LVRGIASQYR YRVVFQGQAA HAGTAMHERR
DALAASAEAI EAIERIGQRD PIDLVTTVGW LSVGAGAPNI VPGRVEFSVD IRAVELDVRE
QAAEHIVAAL REIGARRGIE LEITRTQELT GALCDTRLNT LLDSAIRATA KETPPLLVSQ
AGHDAMIMAH LAPMTMLFIR CAGGISHNPA ESVESVDVEA AHRALVEFVE RFGEAA
//
