ID A0A098EU11_9BACI Unreviewed; 579 AA.
AC A0A098EU11;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=BN1002_00211 {ECO:0000313|EMBL:CEG25401.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG25401.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG25401.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG25401.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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:0000256|ARBA:ARBA00000479};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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DR EMBL; CCXR01000001; CEG25401.1; -; Genomic_DNA.
DR RefSeq; WP_048823182.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098EU11; -.
DR STRING; 1476857.BN1002_00211; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000042335; Unassembled WGS sequence.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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:SF6; ADENINE DEAMINASE YERA-RELATED; 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 {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000042335}.
FT DOMAIN 77..361
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 409..570
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 579 AA; 66499 MW; DF87D66BBCF188CE CRC64;
MEQRYRWKNK HLREHIDVLD GKLAPTILLK NATYLNQTFR SWMKANIWIY DDRIVYVGEK
MPSNLVNCDT IDCTDQYIVP GYIEPHAHPF QLYNPHSFAA YASSRGTTTI INDNMSLVLH
LNKKRAFLLM KDLRSIPATM YWWCRFDPQT EILNEEEVFS HNQIKSWLEH DAVLQGGELT
GWPKLLAGDD MMLHWIQEAK RMRKQIEGHF PGASEKTLAK MMLLGADCDH EAMTGEEVYD
RLMQGYTVSL RHSSIRPDLP RLLDDMKRLG ITAYDNLIFT TDGSSSGFYH EGVIDQMIKI
AIEKGIPVID AYNMATINPA KYYNFAHIHG KIATGRIANL NFLTSMEDPC PVSVLAKGKW
VKRDGANINS FPELDWKEYG LEPLKLDWEL TEDDLQFSMP FGIQMENAVI TKPYSISIEV
SRDQLSDSHD ECFFMLIDRN GKWRVNTLLK GFANKLQGMA SSFSNTGDII LIGKNKADIL
HAFNRMKEIG GGIVVSEGEE AICEIPLRLG GLMTELPLEE LMETERRLQD VLRERGYVYS
DPVYSLLFFS STHLPYIRIT QQGMYDVMNK MVLFPSIMR
//