ID A0A1B7ZEW9_9FLAO Unreviewed; 433 AA.
AC A0A1B7ZEW9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:OBR42106.1};
GN ORFNames=A9200_01575 {ECO:0000313|EMBL:OBR42106.1};
OS Maribacter hydrothermalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR42106.1, ECO:0000313|Proteomes:UP000092164};
RN [1] {ECO:0000313|Proteomes:UP000092164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA Zhan P.;
RL Submitted (JUN-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:OBR42106.1}.
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DR EMBL; LZFP01000001; OBR42106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7ZEW9; -.
DR STRING; 1836467.BTR34_09945; -.
DR OrthoDB; 9769665at2; -.
DR Proteomes; UP000092164; 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:0000313|EMBL:OBR42106.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092164};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..433
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008602638"
FT DOMAIN 231..330
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 433 AA; 46926 MW; DD2B21B856E0BF2E CRC64;
MNMRNFKIII ALFLISNPLL FVNAQISVNQ DRLEKRIIEL AQFGIQENGE TERVAFSDAD
IAAQQWVIEK LKVMDIETHI DFAGNVIGIR KGTDSNMKPI SFGSHIDRVP NGGNYDGCLG
SMAAIEVLQV LNEKKIKTKH PLEIIIFSNE EGGVMGSRAI VGHLNKSALG IKNNTGFTMG
EGVMRLGGDT TRIEQVARKK GDVAAFLELH IEQGGTLEKE NLAIGIVKGI VGLKWWDVEF
NGFANHAGTT PMNARKDALL AASKFIIAVN EIATSFDGAQ VATVGRISAE PGAPNVIPGH
VITSLEIRDL SSVVIEKIYT AIEKRAVEIN EESGVEITFK KLDTTADPAI MDSLIQSEIE
KSIKSLNLSY MFMPSGAGHD AQDMALIAPT GMIFVPSKDG ISHSPKEFTS ASDMANGANV
LLQTILSLDK RLK
//
