Y1085_PICTO
ID Y1085_PICTO Reviewed; 573 AA.
AC Q6L032;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Putative adenine deaminase PTO1085;
DE Short=Adenase;
DE Short=Adenine aminase;
DE EC=3.5.4.2;
GN OrderedLocusNames=PTO1085;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017261; AAT43670.1; -; Genomic_DNA.
DR RefSeq; WP_011177886.1; NC_005877.1.
DR AlphaFoldDB; Q6L032; -.
DR SMR; Q6L032; -.
DR STRING; 263820.PTO1085; -.
DR EnsemblBacteria; AAT43670; AAT43670; PTO1085.
DR GeneID; 2844592; -.
DR KEGG; pto:PTO1085; -.
DR PATRIC; fig|263820.9.peg.1125; -.
DR eggNOG; arCOG00693; Archaea.
DR HOGENOM; CLU_027935_0_0_2; -.
DR OrthoDB; 12286at2157; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..573
FT /note="Putative adenine deaminase PTO1085"
FT /id="PRO_0000142449"
SQ SEQUENCE 573 AA; 65635 MW; 14ABA093C2F7D892 CRC64;
MLLKNIKISN DYNIFMIIAS RKPSLKDIYK IIKVSKFDEP ADLIIEDASY IDIYTKRISS
GNIAIASGRI AYIGDEMPLK NNDTRIIKND FLIAPGYIEG HAHPFQIYNP VTFNEIMIRH
GTSMVISDDL PIYIKMGLKN IKRFMRFMGR LPVKNFWSVR LDSQSMIDME KFSYIKIKEL
LNDDYVLQAG EITGWPYIIN MEKNMLKNIY NSQFLGKRIE THNPGASKNT LNRMAAAGIT
SDHEAITGED VKTRLSLGYH VFLRYSSIRK DLKDELKYII DEKLPLNRLM LTNDGSPYYN
DYMGMDDLIK IAISTGLNPF DAYSMASLNP AVYYNIDGIY GGIAPGRLAD MNFIRDLYNP
EPVFLMLDGK IIDKEVKLDP PDWKGYGMLY KNRNIDINKI NFNGSDETLF MRNQVIMDLN
KYKMEDSMEI HLITKDLKRI VSSNIHGMGQ FDALASSYNI EGSYIVIGSS HDLMKKALKE
VIKNGGIVFN GNKNIRIELK ILGIMSDKHS DDVRNITEEF RSTMRGSGYK FDDPVYSMLF
LNSINLPYYR ITSSGIVEVK TRKIIKKPVS LKI