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Database: UniProt
Entry: Q6A5I4_CUTAK
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Original site: Q6A5I4_CUTAK 
ID   Q6A5I4_CUTAK            Unreviewed;       341 AA.
AC   Q6A5I4;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   OrderedLocusNames=PPA2273 {ECO:0000313|EMBL:AAT83979.1};
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT83979.1, ECO:0000313|Proteomes:UP000000603};
RN   [1] {ECO:0000313|EMBL:AAT83979.1, ECO:0000313|Proteomes:UP000000603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT83979.1; -; Genomic_DNA.
DR   RefSeq; WP_002519568.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A5I4; -.
DR   EnsemblBacteria; AAT83979; AAT83979; PPA2273.
DR   GeneID; 66622162; -.
DR   KEGG; pac:PPA2273; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_0_0_11; -.
DR   Proteomes; UP000000603; 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   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:AAT83979.1}.
FT   DOMAIN          10..337
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   341 AA;  36439 MW;  5F214409E3A1C3A2 CRC64;
     MDSAEAMNLP KVVLHDHLDG GLRPATVLEL AAQRGRPVPA QTPEDLATWF FESADSGSLA
     RYLDAFTETI ALMQDADSLR RVAREFVVDM ATDGVIYAEA RWAPQQHLTG GLSAAEAVEA
     VQVGLVDGME SASLSGTTII ARQILCLMRH LDVPEDVVDL AVNHAPGVVG VDVAGPEDGF
     PLAPFTNALT RVQAAGIHLT VHAGEAAGPE SILDALNHGA ERLGHGVRII EDRDESGWGP
     TAQQVLSNQV PLEVCPTSNT QTGICRKVAE HPLSTLWSTG FNITVSCDNR LMSRTTTSRE
     ISLVSQALCW NRDDALAAQR NALQAAFCSQ DDKQSLVPLL V
//
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