ADDL_TREPA
ID ADDL_TREPA Reviewed; 299 AA.
AC O83085; R9UUU2;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative adenosine/adenine deaminase;
DE EC=3.5.4.-;
DE AltName: Full=Adenosine aminohydrolase;
GN Name=add {ECO:0000312|EMBL:AGN75265.1}; OrderedLocusNames=TP_0045;
GN ORFNames=TPANIC_0045 {ECO:0000312|EMBL:AGN75265.1};
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=24058545; DOI=10.1371/journal.pone.0074319;
RA Petrosova H., Pospisilova P., Strouhal M., Cejkova D., Zobanikova M.,
RA Mikalova L., Sodergren E., Weinstock G.M., Smajs D.;
RT "Resequencing of Treponema pallidum ssp. pallidum strains Nichols and SS14:
RT correction of sequencing errors resulted in increased separation of
RT syphilis treponeme subclusters.";
RL PLoS ONE 8:E74319-E74319(2013).
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; AE000520; AAC65039.1; -; Genomic_DNA.
DR EMBL; CP004010; AGN75265.1; -; Genomic_DNA.
DR PIR; D71374; D71374.
DR RefSeq; WP_010881494.1; NC_021490.2.
DR AlphaFoldDB; O83085; -.
DR SMR; O83085; -.
DR IntAct; O83085; 6.
DR STRING; 243276.TPANIC_0045; -.
DR EnsemblBacteria; AAC65039; AAC65039; TP_0045.
DR EnsemblBacteria; AGN75265; AGN75265; TPANIC_0045.
DR GeneID; 57878586; -.
DR KEGG; tpa:TP_0045; -.
DR KEGG; tpw:TPANIC_0045; -.
DR PATRIC; fig|243276.5.peg.48; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_2_0_12; -.
DR OMA; ANSKSIM; -.
DR OrthoDB; 554648at2; -.
DR Proteomes; UP000000811; 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; Reference proteome; Zinc.
FT CHAIN 1..299
FT /note="Putative adenosine/adenine deaminase"
FT /id="PRO_0000194396"
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
