ID ADEC_ECOSE Reviewed; 588 AA.
AC B6I3P6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=ECSE_3949;
OS Escherichia coli (strain SE11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
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 -!- SUBUNIT: Homodimer. {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; AP009240; BAG79473.1; -; Genomic_DNA.
DR RefSeq; WP_001065694.1; NC_011415.1.
DR AlphaFoldDB; B6I3P6; -.
DR SMR; B6I3P6; -.
DR GeneID; 75205379; -.
DR KEGG; ecy:ECSE_3949; -.
DR HOGENOM; CLU_027935_0_0_6; -.
DR Proteomes; UP000008199; Chromosome.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR01178; ade; 1.
DR PANTHER; PTHR11113:SF2; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese.
FT CHAIN 1..588
FT /note="Adenine deaminase"
FT /id="PRO_1000146238"
SQ SEQUENCE 588 AA; 63735 MW; 273570C5C8594157 CRC64;
MNNSINHKFH HISRAEYQEL LAVSRGDAVA DYIIDNVSIL DLINGGEISG PIVIKGRYIA
GVGAEYADAP 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 LMSTDTAQLL AEQIDALKAA
ARECGPLPDE PFIQMAFLSL PVIPALKLTS QGLFDGEKFA FTTLEVTE
//
