ID   ADEC_RHILO              Reviewed;         605 AA.
AC   Q98NF9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, 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=mlr0157;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
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DR   EMBL; BA000012; BAB47802.1; -; Genomic_DNA.
DR   RefSeq; WP_010909172.1; NC_002678.2.
DR   AlphaFoldDB; Q98NF9; -.
DR   SMR; Q98NF9; -.
DR   STRING; 266835.14021189; -.
DR   EnsemblBacteria; BAB47802; BAB47802; BAB47802.
DR   KEGG; mlo:mlr0157; -.
DR   PATRIC; fig|266835.9.peg.122; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000552; 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; 2.30.40.10; -; 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; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..605
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142431"
SQ   SEQUENCE   605 AA;  64402 MW;  59B8A14CD52995B5 CRC64;
     MAKKPAAHAT KPKPWTEMAT HLVDVAMGRK PADLVIRNGR WVNVHSGEII AGTDIAIAGG
     RFAYCGPNAS HAIGQGTKVV DAGGRYLVPG LCDAHMHVES GMVTVTEFCR AVIPHGTTSM
     FIDPHEIANV LGLPGVRLMH DEAVAMPINV HVQMPSCVPS APGLEHAGAE LTVADVAEAM
     TWENIIGLGE VMNFPGVAAN DPVMSGEIAA TVRAGKTVGG HYASRDLGLP FHGYVAGGPE
     DDHEGTRAED AIARVRQGMK AMLRLGSAWY DVASQIKAVT EGGIDPRNFI LCTDDSHSGT
     LVHEGHMDRV VRHAIQQGLK PVTAIQMATI NTAQHFRLER EIGSIAPGRL ADLLIVSDLA
     AMTIDEVYAR GVRLAKGGKL DIDIPAYDYP KTAKNTVKLG KKLRAGDFDI TAPKGANEVR
     VRVIGVIENQ APTRALEADL PVEDGLVAMD RRNDVCQIAL VERHRGTGGV TNAFVSGFGY
     MGDCAMASSV AHDAHHIICV GTNKQDMALA VNRLGQVGGG VVLFSKGKEL ALVEMPIAGL
     MSDERAEIVA AKAEKLTEAM RKMGCSLNNA YMQHSLLALV VIPELRISDV GLIDVTTFQK
     VDLFV