ID   ADEC_ECOLI              Reviewed;         588 AA.
AC   P31441; P78121; Q2M7X8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Adenine deaminase;
DE            Short=Adenase;
DE            Short=Adenine aminase;
DE            EC=3.5.4.2;
GN   Name=ade; Synonyms=yicP; OrderedLocusNames=b3665, JW3640;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=11440125; DOI=10.1271/bbb.65.1112;
RA   Matsui H., Shimaoka M., Kawasaki H., Takenaka Y., Kurahashi O.;
RT   "Adenine deaminase activity of the yicP gene product of Escherichia coli.";
RL   Biosci. Biotechnol. Biochem. 65:1112-1118(2001).
RN   [5]
RP   CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=12077137; DOI=10.1074/jbc.m204268200;
RA   Petersen C., Moeller L.B., Valentin-Hansen P.;
RT   "The cryptic adenine deaminase gene of Escherichia coli. Silencing by the
RT   nucleoid-associated DNA-binding protein, H-NS, and activation by insertion
RT   elements.";
RL   J. Biol. Chem. 277:31373-31380(2002).
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:0000269|PubMed:11440125, ECO:0000269|PubMed:12077137};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11440125, ECO:0000269|PubMed:12077137};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11440125}.
CC   -!- INDUCTION: Repressed by H-NS. Activated by insertion of a variety of IS
CC       elements into a region extending from -145 to +13 relative to the
CC       transcription start site. IS elements essentially eliminate the H-NS-
CC       mediated silencing, but also stimulate ade expression 2-3 fold
CC       independently of the H-NS protein. {ECO:0000269|PubMed:12077137}.
CC   -!- MISCELLANEOUS: Ade is a cryptic gene in wild-type strains. The
CC       physiological conditions that lead to its activation are unknown.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000305}.
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DR   EMBL; L10328; AAA62017.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76688.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77628.1; -; Genomic_DNA.
DR   PIR; B65168; B65168.
DR   RefSeq; NP_418121.1; NC_000913.3.
DR   RefSeq; WP_001065718.1; NZ_SSZK01000043.1.
DR   AlphaFoldDB; P31441; -.
DR   SMR; P31441; -.
DR   BioGRID; 4262580; 9.
DR   DIP; DIP-12439N; -.
DR   IntAct; P31441; 11.
DR   STRING; 511145.b3665; -.
DR   SWISS-2DPAGE; P31441; -.
DR   jPOST; P31441; -.
DR   PaxDb; P31441; -.
DR   PRIDE; P31441; -.
DR   EnsemblBacteria; AAC76688; AAC76688; b3665.
DR   EnsemblBacteria; BAE77628; BAE77628; BAE77628.
DR   GeneID; 948210; -.
DR   KEGG; ecj:JW3640; -.
DR   KEGG; eco:b3665; -.
DR   PATRIC; fig|1411691.4.peg.3040; -.
DR   EchoBASE; EB1643; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   InParanoid; P31441; -.
DR   OMA; TDHECFT; -.
DR   PhylomeDB; P31441; -.
DR   BioCyc; EcoCyc:EG11692-MON; -.
DR   BioCyc; MetaCyc:EG11692-MON; -.
DR   PRO; PR:P31441; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IDA:EcoCyc.
DR   GO; GO:0004096; F:catalase activity; IDA:EcoCyc.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR   GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..588
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142420"
SQ   SEQUENCE   588 AA;  63739 MW;  2732C6B1B6595E48 CRC64;
     MNNSINHKFH HISRAEYQEL LAVSRGDAVA DYIIDNVSIL DLINGGEISG PIVIKGRYIA
     GVGAEYTDAP ALQRIDARGA TAVPGFIDAH LHIESSMMTP VTFETATLPR GLTTVICDPH
     EIVNVMGEAG FAWFARCAEQ ARQNQYLQVS SCVPALEGCD VNGASFTLEQ MLAWRDHPQV
     TGLAEMMDYP GVISGQNALL DKLDAFRHLT LDGHCPGLGG KELNAYITAG IENCHESYQL
     EEGRRKLQLG MSLMIREGSA ARNLNALAPL INEFNSPQCM LCTDDRNPWE IAHEGHIDAL
     IRRLIEQHNV PLHVAYRVAS WSTARHFGLN HLGLLAPGKQ ADIVLLSDAR KVTVQQVLVK
     GEPIDAQTLQ AEESARLAQS APPYGNTIAR QPVSASDFAL QFTPGKRYRV IDVIHNELIT
     HSHSSVYSEN GFDRDDVSFI AVLERYGQRL APACGLLGGF GLNEGALAAT VSHDSHNIVV
     IGRSAEEMAL AVNQVIQDGG GLCVVRNGQV QSHLPLPIAG LMSTDTAQSL AEQIDALKAA
     ARECGPLPDE PFIQMAFLSL PVIPALKLTS QGLFDGEKFA FTTLEVTE