ID W4F7F1_9BACL Unreviewed; 576 AA.
AC W4F7F1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=C176_00490 {ECO:0000313|EMBL:ETT88823.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT88823.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT88823.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT88823.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT88823.1}.
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DR EMBL; ASQA01000001; ETT88823.1; -; Genomic_DNA.
DR RefSeq; WP_038178691.1; NZ_ASQA01000001.1.
DR AlphaFoldDB; W4F7F1; -.
DR PATRIC; fig|1227360.4.peg.101; -.
DR eggNOG; COG1001; Bacteria.
DR Proteomes; UP000019062; 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:UP000019062}.
FT DOMAIN 76..359
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 406..567
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 576 AA; 65262 MW; 3E3F2F84C29229E2 CRC64;
MPEPSWKISQ IRQQIAIIDG KEAPNLVIKN ARYLHGIYKQ WIQGNIWIDK DRIIYAGSKM
PPNTATTEIV DAEGQTIVPG YIEPHVHPFQ LYNPQSFADY AAQRGTTTFL SDNLMLFLAI
KNKKAFSILE QLKQLPFSFY WWARFDSQTE LENEHDLFTT KAINDWLERT DVMLGGELTG
WPRLLAGDDQ MLYWLKLAKA HGKKIEAHLP GASERTLARM KLFGADGDHE SMTLKEVENR
ILHGYAVTLR HSSIRPDLPI LLKDIVEKKL NIFDHLMMTT DGATPSFHRD GVMDKCIQVA
LDAGVAPIDA YQMASYNVAR YYNMSNLHGL IATGRYATLN FLENEFNPVP VSVLSKGVWL
KRDNKKEFTL PTIDWTAMGT LDLKFDLSDD DFQFSMPFGI QLVNDVITKP YSVSVHTNEG
KLHTDHDECY LMLVDKNGKW RVNTLIKGFA THLQGFASSY SSTGDIILIG KDTKDMLIAF
NEMKKMKGGI VIVENGRVLE SLPLSIGGGL SAEPVEVLIE QELALKKALQ ERGYHLGDAI
YTLLFLQSTH LPYIRITQRG IFDVMKKTVL FPSVMR
//
