ADEC_BRUSU
ID ADEC_BRUSU Reviewed; 581 AA.
AC Q8FW12; G0KD30;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518};
GN OrderedLocusNames=BRA0653, BS1330_II0647;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; EC=3.5.4.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR EMBL; AE014292; AAN33842.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20118.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FW12; -.
DR SMR; Q8FW12; -.
DR EnsemblBacteria; AEM20118; AEM20118; BS1330_II0647.
DR KEGG; bms:BRA0653; -.
DR KEGG; bsi:BS1330_II0647; -.
DR PATRIC; fig|204722.22.peg.2344; -.
DR HOGENOM; CLU_027935_0_0_5; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000007104; Chromosome II.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01178; ade; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese.
FT CHAIN 1..581
FT /note="Adenine deaminase"
FT /id="PRO_0000142411"
SQ SEQUENCE 581 AA; 62746 MW; 34D0C8E60F57B93A CRC64;
MRHCDSFCEL IPMKGCEAML EWMIDQGAGR EPADIVLKGG RFLDLITGEL VESDIAICED
RIVGTFGTYR GKHEIDVSGR IVVPGFIDTH LHIESSQVTP HEFDRCVLPQ GVTTAICDPH
EIANVLGAEG IRFFLDSALE TVMDIRVQLS SCVPATHMET SGVELLIDDL LPFADHPKVI
GLAEFMNFPG VLAKDPECMA KLRAFQGRHI DGHAPLLRGL DLNGYIAAGI RTEHEATNAE
EALEKLRKGM YVLVREGSVS KDLKALMPII TERHAQFLAL CTDDRNPLDI ADQGHLDYLI
RTAIAGGVEP LAIYRAASVS AARAFGLFDR GLVAPGQRAD LVVVDSLEGC HAEIVLSAGR
VVSEALFAAR KPVAEVGRNS VKAPRVTASN FRSQSNSGKT RAIGIVPGKI ITQNLEFDLK
VGPNGVEPDL ERDVVKVAVI ERHGKNGNIA TGFVHGFGLK AGAIASTVSH DSHNICVVGA
SDEDIATAAN RLGEIEGGFV VVRDGKVLAE MPLPIAGLMS TEPYETVREA LRKLRHAAED
LGSVLEEPFL QLAFIALPVI PHLKITDRGL VDVDKFEFVG N