ID A0A0M8JPC1_9CHLR Unreviewed; 587 AA.
AC A0A0M8JPC1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ADN01_16785 {ECO:0000313|EMBL:KPL76209.1}, LSAC_02925
GN {ECO:0000313|EMBL:GAP19027.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:GAP19027.1};
RN [1] {ECO:0000313|EMBL:GAP19027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:GAP19027.1};
RA Matsuura N., Tourlousse M.D., Ohashi A., Hugenholtz P., Sekiguchi Y.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1, Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Class Anaerolineae (Chloroflexi).";
RL Genome Announc. 3:e00975-15(2015).
RN [2] {ECO:0000313|EMBL:KPL76209.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL76209.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) 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; DF967975; GAP19027.1; -; Genomic_DNA.
DR EMBL; LGCM01000064; KPL76209.1; -; Genomic_DNA.
DR RefSeq; WP_062419336.1; NZ_LGCM01000064.1.
DR AlphaFoldDB; A0A0M8JPC1; -.
DR STRING; 229921.ADN01_16785; -.
DR PATRIC; fig|229921.5.peg.1757; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000050501; 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:UP000050501}.
FT DOMAIN 71..355
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 410..577
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 587 AA; 62589 MW; 17326E9C041616A7 CRC64;
MDLTGVRMDL VQAALGRIAF DALILNVQVV NVYSGLVEPG NIGIKHGRIV TCQAPKDAPA
ESIWDGQGRF ALPGLIDTHV HIDSTLLTPA GLAEFMVPHG TTAVFADPME ISNVAGIEGL
KAFFAGSDQL PYHVFLEVCS RVPTAPGLET TGGELGLAEV QEVLAWPQSI SLGELDPSKI
LGLREEYFAK VTAAHALGKI ANGHAAGLSP EALTAYACGG LADDHECVDY AEAKQRVALG
LSVLIREGST ERNLKELVGG LLRENADTRH WMMCTDDKHP NEILHEGHIN YMVEQAIALG
MPPVRAIQMA TLNAAQHFRL DHELGSLAPG RWADILLISS LERIAPEEVF FKGRRVAQNG
KMIIPTPAPA YPDWLHHTVK ITRGLQAEHY RLAAQGAAVR ARVIEITGDQ IINRAGEALL
PVVDGAVQTD PQADVVKLSV VERYGKNGNI GTTFVRGFGL KRGAISSTVS HDHHNLVIAG
ADDLSMATCA RATQEMQGGL VAALGDQVIA QLPLPFGGLI SEAPPLEVIR VLEALNAAAH
SLGCVLPAPF MTLAFISLPT VPELGLTDRG LVDVHQHALI SPLLGLD
//
