ADDL_TREPS
ID ADDL_TREPS Reviewed; 299 AA.
AC B2S1Z3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Putative adenosine/adenine deaminase;
DE EC=3.5.4.-;
DE AltName: Full=Adenosine aminohydrolase;
GN OrderedLocusNames=TPASS_0045;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
CC -!- FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic
CC deamination of adenosine or some similar substrate and play a role in
CC purine metabolism. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9I6Y4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9I6Y4};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; CP000805; ACD70472.1; -; Genomic_DNA.
DR RefSeq; WP_010881494.1; NC_021508.1.
DR AlphaFoldDB; B2S1Z3; -.
DR SMR; B2S1Z3; -.
DR EnsemblBacteria; ACD70472; ACD70472; TPASS_0045.
DR GeneID; 57878586; -.
DR KEGG; tpp:TPASS_0045; -.
DR PATRIC; fig|455434.6.peg.41; -.
DR OMA; ANSKSIM; -.
DR Proteomes; UP000001202; Chromosome.
DR GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT CHAIN 1..299
FT /note="Putative adenosine/adenine deaminase"
FT /id="PRO_1000128871"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9I6Y4"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9I6Y4"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9I6Y4"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9I6Y4"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 208
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 34543 MW; 9717F4430E65B1D8 CRC64;
MKSLEYYRSQ PKADVHTHLN LSMKYERYKQ WSGVVIPNFP RKMRGLDEMH EIIGEYTRPQ
CKTAQDVLNL FTMSIEDAIA DNVVVMETSV DIGFITHYEE NLDHFLCDLS DLHRRYKRNV
TLHFELGISK IRERSFVEQW AEPMMRSGIF ENIDLYGPEI SEGIEDFIYI FKLAEKYHLK
KKAHVGEFSD AQSVRHFVEI FNLDEVQHGI GAATDENVLR FLAERKVRCN VCPTSNVMLN
AVECLEKHPI KKMMDAGVRV GLGTDDLLFF GKTNSEQLFD MVSCGLITEL HAEALLAVR
