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Database: UniProt
Entry: E3FDL6_STIAD
LinkDB: E3FDL6_STIAD
Original site: E3FDL6_STIAD 
ID   E3FDL6_STIAD            Unreviewed;       388 AA.
AC   E3FDL6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   Name=add {ECO:0000313|EMBL:ADO70095.1};
GN   OrderedLocusNames=STAUR_2291 {ECO:0000313|EMBL:ADO70095.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO70095.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO70095.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO70095.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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}.
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DR   EMBL; CP002271; ADO70095.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3FDL6; -.
DR   STRING; 378806.STAUR_2291; -.
DR   KEGG; sur:STAUR_2291; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_0_0_7; -.
DR   Proteomes; UP000001351; Chromosome.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR   CDD; cd01320; ADA; 1.
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   NCBIfam; TIGR01430; aden_deam; 1.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF43; ADENOSINE 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:ADO70095.1}.
FT   DOMAIN          43..367
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  42748 MW;  EF33F6BF689762F1 CRC64;
     MNMASIRDDE LPNATGIPSA ARRTDISPPP ALEVTEELLH ALPKTDLHCH LDGSMRLKTI
     LELAEQQKVK LLADTEDGLA QAIHMGQVCK SLDEYLVAFD VTLSVLQTAE ALYRSAYELA
     VDAAAENVRY LEVRYSPALH LQKGLKMTTV IDSVLEGLRA AKRETGIKYG VIVCGIRHIN
     PQTSMRLAEL SVAYKNRGVI GFDLAGAEAS FPAKDHKDAF QLILKNNVNC TAHAGEAFGP
     ESISQAIHYL GAHRIGHGTR LREDGDLLNY VNDHRIPLEV CPTSNVQTGA VTSLAAHPLK
     FYFDYGLRVT INTDNRLITD TTVTKELWVA HKELGLSLED LTTILVSGFK SAFLPFREKQ
     DLLRSVNQEI ATTLAAFETR PKMVRQPA
//
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