ADEC_BRUA2
ID ADEC_BRUA2 Reviewed; 581 AA.
AC Q2YKR3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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}; OrderedLocusNames=BAB2_0587;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12753.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YKR3; -.
DR SMR; Q2YKR3; -.
DR STRING; 359391.BAB2_0587; -.
DR EnsemblBacteria; CAJ12753; CAJ12753; BAB2_0587.
DR KEGG; bmf:BAB2_0587; -.
DR HOGENOM; CLU_027935_0_0_5; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000002719; 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; Reference proteome.
FT CHAIN 1..581
FT /note="Adenine deaminase"
FT /id="PRO_0000296719"
SQ SEQUENCE 581 AA; 62688 MW; 8FE87E90AE559DF4 CRC64;
MRHCDSFCEL IPMKGCEAML EWMIDQGAGR EPADIVLKGG RFLDLITGEL VESDIAICED
RIVGTFGTYR GKHEIDVSGR IVVPGFIDTH LHIASSQVTP HEFDRCVLPQ GVTTAICDPH
EIANVLGAEG IRFFLDSALE TVMDIRVQLS SCVPATHMET SGAELLIDDL LPFADHPKVI
GLAEFMNFPG VLAKDPECMA KLRAFQGRHI DGHAPLLRGL DLNGYIAAGI RTEHEATNAE
EALEKLRKGM YVLVREGSVS KDLKALMPII TERHAQFLAL CTDDRNPLDI ADQGHLDYLI
RTAIAGGVEP LAIYRAASVS AARVFGLFDR 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