ADEC1_ALKCK
ID ADEC1_ALKCK Reviewed; 576 AA.
AC Q5WJ39;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Adenine deaminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade1 {ECO:0000255|HAMAP-Rule:MF_01518}; Synonyms=adeC;
GN OrderedLocusNames=ABC1077;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD63616.1; -; Genomic_DNA.
DR RefSeq; WP_011245932.1; NC_006582.1.
DR AlphaFoldDB; Q5WJ39; -.
DR SMR; Q5WJ39; -.
DR STRING; 66692.ABC1077; -.
DR EnsemblBacteria; BAD63616; BAD63616; ABC1077.
DR KEGG; bcl:ABC1077; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; TDHECFT; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000001168; 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; 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..576
FT /note="Adenine deaminase 1"
FT /id="PRO_0000142402"
SQ SEQUENCE 576 AA; 61348 MW; DF23D69E3742EDFC CRC64;
MDRHHATYKK RLAAASKQEP ADILVINGKL IDVYTLTIYE ASIAITDGYI VGIGDYTEGK
TVIDAQGKYV CPPLIDGHVH IESAMVRPED FAGVLVPKGV LTAIADPHEL ANVAGVEAVT
YMVEAAKDLP LDIKMAVPSS VPAASFEENG ASLSAEDVRL LFANEGVYGL GEVMDYPAVL
NGDDDMLEKI AMAKAKGRPI DGHAAGLNSD ALNAYRTAGI HNDHEAVTAE EAKARVQRGF
YVLMREGTAA RDIEALLPAV TAANARRFAF ATDDKHLDDL LKEGSVDFNV RKAIALGMDP
LQAIQIGTLN AAECFQLDDK GAIAPGKEAS FLFVSDLSTF QVDAVYAKGM LVAEKGELTS
PIRTPYPVPE RLLNSVHLAP FAREDLTLKL KNAHSTPVIE TTLGSIVTKK AMASVPAENG
IFQPGGKWLK LAVVERHEAT GHIGLAIVKG FPFSEGAIAA TVAHDSHNLI AVGADDESLY
HAIHHVAGLG GGMAVVKGNN VLAAMPLKLG GLMSTDSAET VKQQLNELQQ SLVHLGYQEK
IDPFLTLAFL ALPVIPALKL TSKGLFDVNA FAFVEQ