ID A0A0K9GGU0_9BACI Unreviewed; 581 AA.
AC A0A0K9GGU0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=AC622_18225 {ECO:0000313|EMBL:KMY45903.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY45903.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) 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}.
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:KMY45903.1}.
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DR EMBL; LFZV01000001; KMY45903.1; -; Genomic_DNA.
DR RefSeq; WP_049672348.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9GGU0; -.
DR STRING; 1679169.AC622_18225; -.
DR PATRIC; fig|1679169.3.peg.3908; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000036953; 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:UP000036953}.
FT DOMAIN 78..362
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 411..572
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 581 AA; 66784 MW; 03B1D6E6F2C6340D CRC64;
MLEQRYRWKN KQLREHVSII DGKIAPTIVL VNAVYLNQVF EEWMKANIWI YKDRIIYVGD
KMPDMQEGCE IIDCSGQYLV PGYIEPHAHP AQLYNPETLA MHAAQYGTTT LINDNMTLFT
LLEKRQAFAL LKELRHLPYS MFWWARLDSQ TELRNEEEVF SHANVKSWLE HDGVLQAGEL
TGWPRLLDGD DMMLHWMQEA KRMRKKIEGH FPGSSEKTLA KLMLLGADCD HEAMTGEEVI
RRLGQGYHVS LRHSSIRPDL PGILDYLQDY GLKSYDKCFF NTDGSSPGFY KEGFTDSLIK
MAIDKGVPLI DAYNMASLNI ARYYNMEYLH GNIATGRVAN INFLHEKDEP TPHSVLSKGQ
WVKREGEACG VKGSSINWEE YGLSPLELDW DLTDDDLQYS MPFGINMENS VITKPYSIHI
DISREVLDMN HDECYFTFLR RDGQSRINTL LKGFARNLHG FASSFTNSGD IILIGKSRQD
MKIAFNRMKE IGGGIVIAEK GEILFEMPLV LQGVMSKANL PELIEQESRM KEILVEKGYP
FEDPMYSLLF FTSTHLPYIR VTQAGLYEVM NKSILFPTIM R
//
