ID A0A0M8PQU9_9BACI Unreviewed; 583 AA.
AC A0A0M8PQU9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Adenine deaminase {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000256|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=AN161_26775 {ECO:0000313|EMBL:KOS59915.1};
OS Lysinibacillus sp. FJAT-14222.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1932366 {ECO:0000313|EMBL:KOS59915.1, ECO:0000313|Proteomes:UP000037693};
RN [1] {ECO:0000313|EMBL:KOS59915.1, ECO:0000313|Proteomes:UP000037693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17725 {ECO:0000313|EMBL:KOS59915.1,
RC ECO:0000313|Proteomes:UP000037693};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-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, ECO:0000256|HAMAP-
CC Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773,
CC ECO:0000256|HAMAP-Rule:MF_01518}.
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:KOS59915.1}.
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DR EMBL; LIYL01000065; KOS59915.1; -; Genomic_DNA.
DR RefSeq; WP_053597348.1; NZ_LIYL01000065.1.
DR AlphaFoldDB; A0A0M8PQU9; -.
DR STRING; 1932366.AN161_26775; -.
DR PATRIC; fig|380630.3.peg.882; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000037693; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 71..352
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 406..575
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 583 AA; 63370 MW; 33A219E61A6A8353 CRC64;
MTNKLQQLAQ NILTSQGKIE ADFILRNAQI ADVFTLTWKK ADIVVNNGQI VALDTMNRCK
AKKEEDAAGK YVVPGLIDGH IHIESSMLTP AEFSRVLIPH GITTVLTDPH EIANVAGAEG
IQFMLEDAKK AEMDIFVMLP SSVPGTHFEN AGATLTAADL EPFLKHEDVR GLAEVMDFPA
VLNGEAGMLE KIMLSQQANL VVDGHCAGLN SHQITGYRAA GIHTDHECVT AQEAADRVEQ
GMYVLIREGS AAKNLRDLLP AVNATNARRF GFCTDDKYVD ELMDEGSINF DVAMAIEEGM
EPLQAIQLAT VNTAECYRLY DRGVLAPGYK ADFVLIESID NMRAKAVWKN GVKVAENGAM
LTNRTEPNVP AHIHRSVHLP QVTKDMLSIP FQKGTKANVM EIIPNQLITN HLVIDVPVKD
GVFVPSVEQD LLKLAVIERH HNLHTAGLGI VKGFGLQKGA VATTVAHDSH NALVVGANDE
DMLLALSRIQ EIQGGFVIVA DGEILAEMPL TIGGLMTDVP ADEAKKQLAS LHNALHKLNP
TLDFHFLLTF SFVALPVIPA LKLTDTGLFD VTTFQHIPVE AEV
//
