GenomeNet

Database: UniProt
Entry: R2VL87_9ENTE
LinkDB: R2VL87_9ENTE
Original site: R2VL87_9ENTE 
ID   R2VL87_9ENTE            Unreviewed;       579 AA.
AC   R2VL87;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01518, ECO:0000256|SAAS:SAAS00340006};
DE            Short=Adenase {ECO:0000256|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase {ECO:0000256|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_01518, ECO:0000256|SAAS:SAAS00340006};
GN   Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN   ORFNames=UKC_00474 {ECO:0000313|EMBL:EOI58401.1};
OS   Enterococcus gilvus ATCC BAA-350.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI58401.1, ECO:0000313|Proteomes:UP000013750};
RN   [1] {ECO:0000313|EMBL:EOI58401.1, ECO:0000313|Proteomes:UP000013750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI58401.1,
RC   ECO:0000313|Proteomes:UP000013750};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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_01518,
CC         ECO:0000256|SAAS:SAAS01117456};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenine deaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01518, ECO:0000256|SAAS:SAAS00847022}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EOI58401.1}.
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; AJDQ01000003; EOI58401.1; -; Genomic_DNA.
DR   RefSeq; WP_010778923.1; NZ_KB946867.1.
DR   STRING; 1158614.I592_03887; -.
DR   EnsemblBacteria; EOI58401; EOI58401; UKC_00474.
DR   GeneID; 34362116; -.
DR   PATRIC; fig|1158614.3.peg.485; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000013750; Unassembled WGS sequence.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01518; Adenine_deamin; 1.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR026912; Adenine_deam_C.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000013750};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01518,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01518};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00321440}.
FT   DOMAIN       18     58       Urease_alpha. {ECO:0000259|Pfam:PF00449}.
FT   DOMAIN       67    349       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   DOMAIN      401    571       Adenine_deam_C. {ECO:0000259|Pfam:
FT                                PF13382}.
SQ   SEQUENCE   579 AA;  62529 MW;  A5BC908A450077D5 CRC64;
     MNKKTLKRLI DVAAGRLPAD IVLKNARVID VYQAEIMEGD VAIVDGRIAG IGEAYEGKET
     LDLQGKFVAP GFIDPHIHVE SSYVTPEEFG RLLVPHGTTT VLADPHEIVN VLGLEGLTYM
     VEAAKETALD IRYMMPSCVP ATNMENAGAV IEAEDMIPSF EENHVDGLAE FMNFPGVIHA
     EDSVLDKLLA AKSRGLRIDG HSPMVFAKDL NAYAAAGISN DHECSTVEEL KDRIARGMYV
     FLREGSVTQN LRTLLKGVTE NNYQRCVLSA DDLQAKTMLE KGHLDNSIRI CIEEGVSPIR
     AIQMATINAA QCCQLSDRGA VAPGLRADLV IFSDLTNPTI EATYIAGELI AENGAYLPTV
     NRISTEQVQS SVHINKFQPE QLALTLTSDN ARAIEVIPQE ALTNEAIVSV KRDENNHFVF
     DPSQDVTKIA VIERHHDTGN VFVGLLKEYG LKKGAIGLSI AHDSHNLIVT GTTDEDMAAA
     VHALKEQEGG VVLVESGKVI GSMALPIAGL MSDLSGEAVA KQEAEINHLA HHVLGVSEKV
     DPIMTLGFMS LAVIPNLKIT DIGLVDVTKF EIVPVSVEA
//
DBGET integrated database retrieval system