ID   ADDL_OPITP              Reviewed;         330 AA.
AC   B1ZYW1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative adenosine/adenine deaminase;
DE            EC=3.5.4.-;
DE   AltName: Full=Adenosine aminohydrolase;
GN   OrderedLocusNames=Oter_3003;
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX   PubMed=21398538; DOI=10.1128/jb.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
CC   -!- FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic
CC       deamination of adenosine or some similar substrate and play a role in
CC       purine metabolism (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
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DR   EMBL; CP001032; ACB76284.1; -; Genomic_DNA.
DR   RefSeq; WP_012375813.1; NC_010571.1.
DR   AlphaFoldDB; B1ZYW1; -.
DR   SMR; B1ZYW1; -.
DR   STRING; 452637.Oter_3003; -.
DR   PRIDE; B1ZYW1; -.
DR   EnsemblBacteria; ACB76284; ACB76284; Oter_3003.
DR   KEGG; ote:Oter_3003; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_0; -.
DR   OMA; NHFTIHA; -.
DR   OrthoDB; 554648at2; -.
DR   Proteomes; UP000007013; Chromosome.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43114; PTHR43114; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT   CHAIN           1..330
FT                   /note="Putative adenosine/adenine deaminase"
FT                   /id="PRO_1000128853"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            211
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  36703 MW;  C237C4236D622BF2 CRC64;
     MKLSDFIQAL PKTETHLHVE GALPYELLQA WKPEEYPPNP AFRQPDYRYA TFPDFDSILL
     SHALPWFTNA ERYYEASKAI FAKHVAQNVR YVETSFHLAV TKFIRLPGPE IIAAIRAAVP
     AGLEVRIFTG MLRSDIVGDL RPTIDQLHTW DGLAGVDLHG FEAMRTEPET AAIWARLRAA
     GKITKCHAGE FGGADRVREA IEQLGVDRIQ HGVRAIEDPA VVRLAAERGV TFDMCPISNL
     RLQVVPSLRE HPIRRFMAAG VRCTVSTDDP LNFANTVNDE YHVLASELDF TRAELSQVAR
     NGWAVADVPV AMKRAVSGEI DQLLNGSTPA