(data stored in ACNUC29543 zone)

SWISSPROT: B2JRM0_PARP8

ID   B2JRM0_PARP8            Unreviewed;       341 AA.
AC   B2JRM0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01962};
DE            Short=ADE {ECO:0000256|HAMAP-Rule:MF_01962};
DE            EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_01962};
DE   AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_01962};
DE            Short=AAH {ECO:0000256|HAMAP-Rule:MF_01962};
GN   OrderedLocusNames=Bphy_3185 {ECO:0000313|EMBL:ACC72347.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72347.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC       hypoxanthine. Plays an important role in the purine salvage
CC       pathway and in nitrogen catabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_01962}.
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;
CC         EC=3.5.4.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01962};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01962};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01962};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenosine and AMP deaminases family. Adenine
CC       deaminase type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_01962,
CC       ECO:0000256|SAAS:SAAS00846939}.
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DR   EMBL; CP001044; ACC72347.1; -; Genomic_DNA.
DR   STRING; 391038.Bphy_3185; -.
DR   EnsemblBacteria; ACC72347; ACC72347; Bphy_3185.
DR   KEGG; bph:Bphy_3185; -.
DR   eggNOG; ENOG4105EKD; Bacteria.
DR   eggNOG; COG1816; LUCA.
DR   HOGENOM; HOG000218813; -.
DR   KO; K01488; -.
DR   BioCyc; BPHY391038:G1GBS-3282-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01320; ADA; 1.
DR   HAMAP; MF_01962; Adenine_deaminase; 1.
DR   InterPro; IPR001365; A/AMP_deaminase_dom.
DR   InterPro; IPR028892; ADE.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JRM0.
DR   SWISS-2DPAGE; B2JRM0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01962,
KW   ECO:0000256|SAAS:SAAS00331575, ECO:0000313|EMBL:ACC72347.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01962,
KW   ECO:0000256|SAAS:SAAS00331580};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01962, ECO:0000256|SAAS:SAAS00331599}.
FT   DOMAIN       11    328       A_deaminase. {ECO:0000259|Pfam:PF00962}.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   METAL        17     17       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   METAL        19     19       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   METAL       197    197       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   METAL       278    278       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   BINDING     279    279       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01962}.
FT   SITE        221    221       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01962}.
SQ   SEQUENCE   341 AA;  38371 MW;  5250314834681BA2 CRC64;
     MPTMQTYING LPKAELHMHL EGCIEPDMMF TLAERNGHSL RWPSAEALRS AYEFNDLQSF
     LDLYFEGCHV LVEEQDFYDV THRYLQKAHE QTVRHAEMFT GPQTFTERGT PLEAVMEGVL
     GAMQNAKHEF GITSGLLISA HRHRTQEAAI ELLDSIQPWR ENISGIGMGG AELPNPPSKF
     VEFFARCRAQ NLPVTIHAGE EGPADYIRQA IDLLHVNRID HGNACLTDPS LVRELAERRI
     PLTVCPLSNL KLNVVPSDVP HPLRGMLDAG LCATINSDDP PYFGGYVNEN FAYVQRNLKL
     TRNELVQLAK NSFEASFIDR ALAQRYIDSV DAYDRSVAHI N
//

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