ID I3TCN6_THEC1 Unreviewed; 589 AA.
AC I3TCN6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=TCELL_0099 {ECO:0000313|EMBL:AFK50524.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50524.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK50524.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(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; CP003531; AFK50524.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TCN6; -.
DR STRING; 1184251.TCELL_0099; -.
DR KEGG; thg:TCELL_0099; -.
DR eggNOG; arCOG00693; Archaea.
DR HOGENOM; CLU_027935_0_0_2; -.
DR InParanoid; I3TCN6; -.
DR Proteomes; UP000005270; 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 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|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000005270}.
FT DOMAIN 70..356
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 413..575
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 589 AA; 65235 MW; 10DA78EC17ED5AED CRC64;
MLFLVRSLIE YFEAAAGRRR PTLLLKNARI VDVFTGSVVE GNLEIYKDRI IGLTKRVRDA
DLVLDVKGHY LLPGFIDSHI HIESTLLVPQ QLARLLIPHG VTTLMADPHE IANVLGVRGV
RLLVEMSRMS KIRVFVQVPS RVPTAPGLET TGAVLEDRDV EELLREESAV SLGELNYQNI
LRDPGYLRRV EAALKLGKRS NGHMAGVVEE DFVNALASAV LTDDHEVVSG DEAFVKLVRG
VAVMVREGSS ERNLTDVVKG LVGRLRDYRQ LMFCTDDKHP TDILREGHID YNVRKSIEEG
LDPIVAVQMA TINPATYFRL DHLIGSLAPG RKADVLVVDS LEKLGIRTVV FDGETVYHEG
RLMFEVPRVE LPEWARNTVR VNQGLKAEDL VVKVGSESRK ALVRVIGVIP GQILKKELRE
WLGVRSGVVI GDVGRDIIHI AVVERHKGLP NVGKGFVRGF GLKKGAIGSS VSHDHHNIVV
VGVDPLDMYV AVRRLSEIGG GFVAVMGGEI LAELPLEFAG LMSTRSYEEV VERLNRLEYI
ARHVLGLSLP NPFMQLEFVS LPSVPEIGIT DRGLVVDYKL VDPVIEVYR
//