ADDE_HELPY
ID ADDE_HELPY Reviewed; 409 AA.
AC O25046;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Adenosine deaminase;
DE EC=3.5.4.4;
GN OrderedLocusNames=HP_0267, C694_01350;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=23825549; DOI=10.1371/journal.pone.0066605;
RA Choi H.P., Juarez S., Ciordia S., Fernandez M., Bargiela R., Albar J.P.,
RA Mazumdar V., Anton B.P., Kasif S., Ferrer M., Steffen M.;
RT "Biochemical characterization of hypothetical proteins from Helicobacter
RT pylori.";
RL PLoS ONE 8:E66605-E66605(2013).
CC -!- FUNCTION: Catalyzes the deamination of adenosine into inosine. Is also
CC able to deaminate adenine, but with considerably less efficiency. Is
CC not active toward 6-chloroadenine. {ECO:0000269|PubMed:23825549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000269|PubMed:23825549};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for adenosine {ECO:0000269|PubMed:23825549};
CC KM=2.04 mM for adenine {ECO:0000269|PubMed:23825549};
CC Note=kcat is 1101 min(-1) and 0.47 min(-1) with adenosine and adenine
CC as substrate, respectively.;
CC pH dependence:
CC Optimum pH is about 7.5. Retains > 70% maximum activity at pH 9.0,
CC but displays only 6% activity at pH 4.5.
CC {ECO:0000269|PubMed:23825549};
CC Temperature dependence:
CC Optimum temperature is about 45 degrees Celsius.
CC {ECO:0000269|PubMed:23825549};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07333.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV41491.1; -; Genomic_DNA.
DR PIR; C64553; C64553.
DR RefSeq; NP_207065.1; NC_000915.1.
DR RefSeq; WP_001155847.1; NC_018939.1.
DR AlphaFoldDB; O25046; -.
DR SMR; O25046; -.
DR DIP; DIP-3371N; -.
DR IntAct; O25046; 1.
DR MINT; O25046; -.
DR STRING; 85962.C694_01350; -.
DR PaxDb; O25046; -.
DR EnsemblBacteria; AAD07333; AAD07333; HP_0267.
DR KEGG; heo:C694_01350; -.
DR KEGG; hpy:HP_0267; -.
DR PATRIC; fig|85962.47.peg.287; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_10_1_7; -.
DR OMA; CNEKCEV; -.
DR PhylomeDB; O25046; -.
DR SABIO-RK; O25046; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..409
FT /note="Adenosine deaminase"
FT /id="PRO_0000424561"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 45541 MW; 211A4736AAB1527F CRC64;
MQEIIGASLV FLCNEKCEVL EDYGVVFDEK IVEIGDYQSL TLKYPHLKAQ FFENSVLLPA
FINAHTHFEF SNNKASFDYG SFSGWLGSVL NNGGAILENC QGAIQNAIST QLKSGVGSVG
AISNHLIEVN LLKESPLNAV VFLEFLGSSY SLEKLKAFEA KFKELKDLED KKLKAALAVH
APYSVQKDMA LSVIQLAKDS QSLLSTHFLE SLEELEWVEN SKGWFENFYQ HFLKESHFKS
LYKGANDYID MFKDTHTLFV HNQFASLEAL KRIKSQVKNA FLITCPFSNR LLSGQALDLE
RTKEAGLSVS VATDGLSSNI SLSLLDELRA FLLTHNMPLL ELAKIALLGA TRHGAKALAL
NNGEIEANKR ADLSVFGFNE KFTKEQAILQ FLLHAKEVEC LFLGGKRVI
