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Database: UniProt
Entry: A0A2Y9B9I2_9FIRM
LinkDB: A0A2Y9B9I2_9FIRM
Original site: A0A2Y9B9I2_9FIRM 
ID   A0A2Y9B9I2_9FIRM        Unreviewed;       593 AA.
AC   A0A2Y9B9I2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=A8806_101539 {ECO:0000313|EMBL:PWJ32251.1},
GN   SAMN05216536_101539 {ECO:0000313|EMBL:SSA54084.1};
OS   Faecalicatena orotica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Faecalicatena.
OX   NCBI_TaxID=1544 {ECO:0000313|EMBL:SSA54084.1, ECO:0000313|Proteomes:UP000251306};
RN   [1] {ECO:0000313|EMBL:SSA54084.1, ECO:0000313|Proteomes:UP000251306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:SSA54084.1,
RC   ECO:0000313|Proteomes:UP000251306};
RA   Cai Z.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PWJ32251.1, ECO:0000313|Proteomes:UP000245845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:PWJ32251.1,
RC   ECO:0000313|Proteomes:UP000245845};
RA   Kelly W.;
RT   "The Hungate 1000. A catalogue of reference genomes from the rumen
RT   microbiome.";
RL   Submitted (MAY-2018) 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}.
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DR   EMBL; QGDL01000001; PWJ32251.1; -; Genomic_DNA.
DR   EMBL; UETE01000001; SSA54084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Y9B9I2; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000245845; Unassembled WGS sequence.
DR   Proteomes; UP000251306; 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|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:UP000245845}.
FT   DOMAIN          73..360
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          416..580
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   593 AA;  64954 MW;  1A983B92236DEC13 CRC64;
     MERTIANLKE MIRAGRGIIP ADTVVKGGNL VNVMTSEIYP ADVAIYKDMI AAVGDVSDYT
     GPGTKIIDAE GKYLVPGLID GHIHSECSKL SITSFAKAVV PCGTTSMISG LDEYISVSGL
     EGLKEVLAEV KQSPLKVFWG APYKTPYTIP ESTVSFNFTK EVHEEVQQWP ECFGVWETVR
     EFLQEEDENT LGAIEQAFKN RLPVFGCAPM ARGNDLNGYL CGGVRLDHES YDHEEVVEKM
     RKGMHMLIRE SSVTHFLAEN IRAVTEVNPY MARRVSFCTD DVTATDVLEK GHLDNVVRLA
     IAAGVEPMTA IQMGTINSAE AYRIDHLVGS ISPGRIADIL LVDSPEEFHV ETVITNGQLV
     AQNKKLTYDL KAPERSTVLK SELKCQKTTK ADFEYRVDMI NGTADVLAMD VQGPFVRKRR
     DVVLNVEDGI ILPDPEQDVA LVSVLERFGR NGNRSLAFCS GWNLKRGAMA SSAAPDDNNL
     IVMGVNPEDM SLAVNYLIEQ GGGQVVVADG EIIEFLPLPV GGIASDEEPE VIAAQEKKLN
     KAAQDLGSTL PEPLMYMFFL PITAIPDYAI TDVGPVDYTN LTTFDPVIKL NEQ
//
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