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Database: UniProt
Entry: S9QDA2_9RHOB
LinkDB: S9QDA2_9RHOB
Original site: S9QDA2_9RHOB 
ID   S9QDA2_9RHOB            Unreviewed;       349 AA.
AC   S9QDA2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:EPX79411.1};
DE            EC=3.5.4.4 {ECO:0000313|EMBL:EPX79411.1};
GN   ORFNames=thalar_02236 {ECO:0000313|EMBL:EPX79411.1};
OS   Litoreibacter arenae DSM 19593.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79411.1, ECO:0000313|Proteomes:UP000015351};
RN   [1] {ECO:0000313|Proteomes:UP000015351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX   PubMed=24501650; DOI=10.4056/sigs.4258318;
RA   Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT   member of the Roseobacter clade isolated from sea sand.";
RL   Stand. Genomic Sci. 9:117-127(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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:EPX79411.1}.
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DR   EMBL; AONI01000010; EPX79411.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QDA2; -.
DR   STRING; 1123360.thalar_02236; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_1_5; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000015351; Unassembled WGS sequence.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR   PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EPX79411.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015351}.
FT   DOMAIN          12..335
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   349 AA;  39349 MW;  D994EC5AC5CD1603 CRC64;
     MILSDAYFAA LPKVDIHCHL LGTIREETLW DLAQQARAPI TRDEVADYFI RGEKPRGVLH
     AFRFMEEYVL TTPACLHRLT AECLEDMARE NVLHAELFWN STGTLAHHPS LDFAELQDAI
     TRAMAEAEVA HGITARLIHA IDREASPEDG AATVARTLAH SDPRAVGIGS DYLETGNPPE
     KFWKAYRMAR DGGLKTTMHA GEFGCHWRNI ETAVDLLRVD RLDHCYTILD NPTLLERVRD
     AGIVVTVVPT NSYYMRTLSR DEWAEKHPLR RMLSSGLRLH PNTDDPTFHN TTPNRVWTSI
     HRDFGATTDQ IEAMIWNGVA GAWLDDATRV ALEDRTRRGL EDAKAHLVA
//
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