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Database: UniProt
Entry: U2V4V9_9ACTN
LinkDB: U2V4V9_9ACTN
Original site: U2V4V9_9ACTN 
ID   U2V4V9_9ACTN            Unreviewed;       603 AA.
AC   U2V4V9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=HMPREF1316_1948 {ECO:0000313|EMBL:ERL10387.1};
OS   Olsenella profusa F0195.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=1125712 {ECO:0000313|EMBL:ERL10387.1, ECO:0000313|Proteomes:UP000016638};
RN   [1] {ECO:0000313|EMBL:ERL10387.1, ECO:0000313|Proteomes:UP000016638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0195 {ECO:0000313|EMBL:ERL10387.1,
RC   ECO:0000313|Proteomes:UP000016638};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERL10387.1}.
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DR   EMBL; AWEZ01000010; ERL10387.1; -; Genomic_DNA.
DR   RefSeq; WP_021725119.1; NZ_AWEZ01000010.1.
DR   AlphaFoldDB; U2V4V9; -.
DR   STRING; 1125712.HMPREF1316_1948; -.
DR   PATRIC; fig|1125712.3.peg.328; -.
DR   eggNOG; COG1001; Bacteria.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000016638; 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   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|HAMAP-Rule:MF_01518};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016638}.
FT   DOMAIN          84..372
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          429..595
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   603 AA;  64586 MW;  2463C50F585C4860 CRC64;
     MINSYCKKPL WECNGTLVRV AQGQQAADTV IKDVRLVSVT THEVLERTDI ALSCGRVAYL
     GIDGHSADHC IGAGTTVVDA HGLYATPGLL DSHIHIESSM VGPSEYARAV VPHGTTGLYA
     DPHEVANVRG LEGVRAMWAD AARTPLKAML TTPSCVPAVT GVEDTGADIG AADVAQTMAW
     SETCALGEMM NFPGVLSCEE RPLDEIRETL RADRVVTGHY VSADTDRGLN AYVASGVSSC
     HESGSFDEVL AKLRLGMHAQ LRQGSAWLNL PGYLPRLIES GVDTRLCMLC TDDSHPHTIV
     GDGHMDRVLR TAVGLGLDPV TAVQMATTNT ATYFGVGRDM GAVVPGACAD IVLWDDLKDF
     RARMVWIDGE LVAQDGRALF EVGPFAWPMF MTNTMELGDL LTPEAFQFAC DRPDGHCMVH
     AIEVNAGDTI TRDAIVEVPV HDGLLQADPA HDILKLCVFD RHHGGAGTYS HGFATGFGVH
     GALAQTVSHD AHNLLVMGDN DADMLLAART LEACGGGEVA VQEGRVLALV ELPVCGLMSD
     KPVEVVSDEV SRIEEAWRQM GCRLPSPFMT MGVMSLACVP VLRQTNRGYV NCTTFETEPL
     IAD
//
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