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Database: UniProt
Entry: G7VY73_PAETH
LinkDB: G7VY73_PAETH
Original site: G7VY73_PAETH 
ID   G7VY73_PAETH            Unreviewed;       575 AA.
AC   G7VY73;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=HPL003_05455 {ECO:0000313|EMBL:AET57856.1};
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=985665 {ECO:0000313|EMBL:AET57856.1, ECO:0000313|Proteomes:UP000005876};
RN   [1] {ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AET57856.1, ECO:0000313|Proteomes:UP000005876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003 {ECO:0000313|EMBL:AET57856.1,
RC   ECO:0000313|Proteomes:UP000005876};
RX   PubMed=22328761; DOI=10.1128/JB.06668-11;
RA   Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA   Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT   "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT   Bacterium Isolated from Soil Found in Forest Residue.";
RL   J. Bacteriol. 194:1266-1266(2012).
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}.
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DR   EMBL; CP003107; AET57856.1; -; Genomic_DNA.
DR   RefSeq; WP_014278607.1; NC_016641.1.
DR   AlphaFoldDB; G7VY73; -.
DR   STRING; 985665.HPL003_05455; -.
DR   KEGG; pta:HPL003_05455; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000005876; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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   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          55..339
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          396..560
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   575 AA;  63898 MW;  2E27A1648DEAFB86 CRC64;
     MRADKMILQV KVYNSYYKTF EEGNVAILDG KFMYIGQRGL ESFEVNEIVE GHGKYMIPGL
     IDIHLHIEST MVTPATFSYG LIRNGVTTIV PEPHEMANVF GLEGIQEMMA ASKECVADMF
     YGIPSSVPAT PLETSGGEID IPEIDALLQT GEMICLGEIM NYVDVIRDPE GKTNRILRHV
     REHYPELIIE GHTPQLLDLD LHQLIYAGIG SDHTHQSIEG MKARMAAGMF IEIQEKSMTP
     EVMEYLIQED VAQHFCFVTD DVMPDSFVER GHLNHIVSKA IGMGMKPEDA IYAATFTPAT
     RMRMHDRGTI APGKIADFVL LSDLSHFEVE RVYKDGQKVF DRFEEYHQAS LSSRFPPHFY
     QSVKLKPLTE QDFTVELDVA DGTHHCRIMM VKDGSTFTSE RIAPEQVANG ELMWEQSEHG
     LIATFERYGK NGNRAYGLIG GDTIKRGAVA TTYSHDNHNL LVVGHNKQDM ILAANTVLSS
     QGGFCVVENG KVLSHLPLTV GGILTEGPLE MVAAHVKELR SALLSLGYRH YNPIMSLSTH
     SLPVSPALKI TDHGLIDVNA GKIVSLIVDP SEIQE
//
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