ID A0A1Y4H7C5_9FIRM Unreviewed; 567 AA.
AC A0A1Y4H7C5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=B5F36_07460 {ECO:0000313|EMBL:OUP03845.1};
OS Anaerofilum sp. An201.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerofilum.
OX NCBI_TaxID=1965588 {ECO:0000313|EMBL:OUP03845.1, ECO:0000313|Proteomes:UP000195817};
RN [1] {ECO:0000313|Proteomes:UP000195817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An201 {ECO:0000313|Proteomes:UP000195817};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP03845.1}.
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DR EMBL; NFJT01000010; OUP03845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4H7C5; -.
DR Proteomes; UP000195817; 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 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:UP000195817}.
FT DOMAIN 67..346
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 396..562
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 567 AA; 60110 MW; A057B96D7CA2354B CRC64;
MQQDLLRRLM QVATHERPAR RVLKGGQVLN VFTGRLLDAD VAIEEGIIAA VGPDYAGEEE
IDCTGLTIIP GLIDAHLHIE SAMVQPAELA KVLLPRGTTT LIADPHELAN VSGEAAMDYL
FGAAETCGLN VFVMAPSAVP ASPFDRNGAG VIGASRLAAW KDRALGLGEV MCFPQVVAGD
PAALDKLDAY AGRPIDGHAP GLRGPALQAY RLAGIQTEHE ASDFAEGLEK LEAGFALLVR
EGSAAHNLEP LVTGLLKHRI PTGRCAFCTD DKHLADIFTQ GHIDHCVRRA IELGMPFAQA
VQMATIQPAR IYGLNDLGAV APGCRADLVL LENAARMTIR AVYKDGVPAA ERLADAQAFP
VPDSLLHTVK LPALTEEDLA LYCAAETDAI QPVPRQLLTR RVRASVQRDG AGRFLPDARY
CKLCAVQRHS GEKRLAVAPL EGFGIRGGAL ATTVAHDSHN IVAAGDNDAD LLAAMRALAE
AGGGYAIARG GEVHLLPLPV CGLVSLESGE AVARHTDEML AIAREMGIPA GVDPFITLSF
LSLPVIPAVR LLDGGLFDAE NFRWIVQ
//
