ADEC2_RHIL3
ID ADEC2_RHIL3 Reviewed; 595 AA.
AC Q1MCF8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=RL3883;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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}.
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; AM236080; CAK09373.1; -; Genomic_DNA.
DR RefSeq; WP_011653318.1; NC_008380.1.
DR AlphaFoldDB; Q1MCF8; -.
DR SMR; Q1MCF8; -.
DR STRING; 216596.RL3883; -.
DR EnsemblBacteria; CAK09373; CAK09373; RL3883.
DR KEGG; rle:RL3883; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_5; -.
DR OMA; IEGHFPG; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Hydrolase; Manganese.
FT CHAIN 1..595
FT /note="Adenine deaminase 2"
FT /id="PRO_0000292395"
SQ SEQUENCE 595 AA; 62817 MW; 54D0D1C8F6DC3D5B CRC64;
MNATARQEPA DLNDPALRAR AVTAARGDAP FDMLITGGRL LDTVTGLIRQ ADIGLVGALI
SSVHAPASRT DAVEIIDAAG SILTPGLIDT HMHIESSMVT PAEYASAVLP RGVTTIVWDP
HEFGNVHGLD GVRWAIEAAR SLPLRMILLA PSCVPSAPGL ELAGADFDAS MITEMLHSSA
VGGVAEVMNM RGVIDGDPRM TDIVNAGLAA GKLVCGHARG LEGADLNAFM ASGITSDHEL
TSGADLLAKL SAGLTIELRG SHDHLLQEFV EVLSGLGHLP PTVTLCTDDV FPDELQEGGG
LDDVVRRLVR YGMKPEWAIR AATFNAAQRL KRSDLGLVAT GRRADIVLFE DLTEFRARLV
ISGGRIVARN GSMQVAVQQI DTAPLVNSVK LPPLTENDFR IPAKGERVRV ATIDRPRFTQ
WGEAETEVRD GFIVPPAGSA MISVAHRHGK TDGIPRIGFL TGWGEWRGAF CTTVSHDSHN
LTVFGGNAGD MALAANAVIS AGGGMAVAKD GRIEAMLPLP LSGLVTDASL KDTALAFAGI
RKAMEKIVTW KPPYLVFKAC FGATLACNVG PHQTDQGIAD VVTGKVLENP VLAVW