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Database: UniProt
Entry: A0A099RU31_9CLOT
LinkDB: A0A099RU31_9CLOT
Original site: A0A099RU31_9CLOT 
ID   A0A099RU31_9CLOT        Unreviewed;       562 AA.
AC   A0A099RU31;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=DP68_17140 {ECO:0000313|EMBL:KGK83849.1};
OS   Clostridium sp. HMP27.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK83849.1, ECO:0000313|Proteomes:UP000030009};
RN   [1] {ECO:0000313|EMBL:KGK83849.1, ECO:0000313|Proteomes:UP000030009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMP27 {ECO:0000313|EMBL:KGK83849.1,
RC   ECO:0000313|Proteomes:UP000030009};
RA   Tan B.F., Foght J., Budwill K.;
RT   "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT   degrading methanogenic culture.";
RL   Submitted (APR-2014) 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:KGK83849.1}.
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DR   EMBL; JMFY01000045; KGK83849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099RU31; -.
DR   STRING; 1487921.DP68_17140; -.
DR   eggNOG; COG1001; Bacteria.
DR   Proteomes; UP000030009; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030009}.
FT   DOMAIN          61..341
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          388..553
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   562 AA;  62652 MW;  A727072D653A46ED CRC64;
     MKSNIKIAAR KEKAPLVLKN AFFLNVFTRE FEKGDIAINN GIIAGIGSYE GIEEINCDGL
     FVTPGLIDAH VHIESSKAIP EIFSQVLLQN GVTTCITDPH EIANVLGEKG LDFMMENSKK
     SLMDIFYMIP SCVPATEFED NGALLRSEDI ESYRDRENVI GLAEVMDVPS VVNCTEWILK
     KINMYKDKTI DGHCPQISEE WLNAYIAAGV KTDHECSDAM QALEKVKKGM YVMIREGSAA
     KNLLSLLPAV NEKNYSRFLF CTDDKDIGDL IEKGSINENI KLSIEHGLDE IIAYTIASYN
     AAQCYNLKDR GAIGPGYKAD LVILSDLKKV IIDKVIKSGR VYNHKFDFKG TNPNLQNSMN
     LDVVTEESFK IKAKSSKINV IKVIENSIET KKEEREVIIQ NGYVNSVKGE DILKIAVFER
     HKNTGKYSLG YIEGLGLTEC SVAQTIAHDS HNVIVVGSLD SDMALAVNRL IEIGGGIVLV
     SNGKVIEELE LPIAGLMTYK EPSYVIDKLS NMNSFIKTHE KYEDKDIFLT LGFMALPVIP
     ELKITARGLF YFKDYKFIDL FC
//
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