ID   A9WE92_CHLAA            Unreviewed;       346 AA.
AC   A9WE92;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 96.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:ABY33752.1};
DE            EC=3.5.4.4 {ECO:0000313|EMBL:ABY33752.1};
GN   OrderedLocusNames=Caur_0504 {ECO:0000313|EMBL:ABY33752.1};
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Chloroflexineae; Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY33752.1, ECO:0000313|Proteomes:UP000002008};
RN   [1] {ECO:0000313|Proteomes:UP000002008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC   {ECO:0000313|Proteomes:UP000002008};
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(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; CP000909; ABY33752.1; -; Genomic_DNA.
DR   RefSeq; WP_012256408.1; NC_010175.1.
DR   AlphaFoldDB; A9WE92; -.
DR   STRING; 324602.Caur_0504; -.
DR   EnsemblBacteria; ABY33752; ABY33752; Caur_0504.
DR   KEGG; cau:Caur_0504; -.
DR   PATRIC; fig|324602.8.peg.572; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_0; -.
DR   InParanoid; A9WE92; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:UniProtKB-ARBA.
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; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABY33752.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          14..335
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   346 AA;  37902 MW;  8402983C35307F84 CRC64;
     MLTAELAAFI ERMPKVELHL HLEGAVMPQT FLALSRRNNI SLPVQTEEEL LALFHYDDFH
     NFLETFMALA ATIVSGEDFE LLAFELGMAL ARQYVAYAEV MISPMQHVRR GVDLREALAG
     AASGFARARR QGGPHVGIVL DYGRQYGAEA AWPILETAIA CRSLGVVGWS IGGNEIGHPP
     EEFAELFAAA RRAGLGLMAH AGEVVGPASV WGAIDVLEVS RIGHGIRSVE DPLLLKALAE
     RDVVLDVCPS SNIRTKAVTS WQTHPLRQLY NAGVPVTINS DDPTFFETTL SEEFRRIAHH
     FGFTADDFCR MTLTAVRATF LSPAERDALL TTVAQEQQRL RAALGV
//