ID ADEC_BDEBA Reviewed; 586 AA.
AC Q6MJY0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Bd2636;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX842653; CAE80429.1; -; Genomic_DNA.
DR RefSeq; WP_011165032.1; NC_005363.1.
DR AlphaFoldDB; Q6MJY0; -.
DR SMR; Q6MJY0; -.
DR STRING; 264462.Bd2636; -.
DR KEGG; bba:Bd2636; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_7; -.
DR Proteomes; UP000008080; Chromosome.
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; Manganese; Reference proteome.
FT CHAIN 1..586
FT /note="Adenine deaminase"
FT /id="PRO_0000142405"
SQ SEQUENCE 586 AA; 63714 MW; 95757416BD3FDC62 CRC64;
MSLSNKKTQK IASDLLPARL SQARGDGTLD LLITNVQMLD VITGDIYPTC IAIGGEHIVG
VGMEYQTQSA RRTWNALGAF VTPGFIDGHL HIESSMMSPF EFEKATLPLG TTTAICDPHE
ITNVLGGRGF SWFLRSSELM HQNLFVQMSS CVPALPGFET TGSDFPLEEM KSFKDHPSVL
GLAEMMNFPG VIHADEEVLA KIEAFDDLNM DGHAPLLRGK ALNAYLLAGI QNCHETVTLE
EGREKLQKGM GLIIREGSVA KNLRTLAPLV NEFSSPQCLL CTDDRNPFEI AHEGHINYLI
KELINKHGVA VHVAYRLATY SAARHFGLKR LGLVAPGKKA DLVFLKDLKA VDIQEVMIGG
KFVSELKLQD SLQEKLQTSQ PPLENTMKRS PLTEKELTVN LLPGVYNVIE IVPHEIITQH
LTVAFDGQKF AESDVLYMAN IERYGKGLPP ALGLVKGMGL KSGALASSVA HDSHNIMVIG
TNPADMVLAV NTLIKSGGGF AVADQGEIKA LVELPIAGLL SLKSAEEIKD GIADLKTAFR
SLGVHLDEPF IQMAFLALPV IPTLKLTDRG LVNVTNFSFI PLQVEA
//
