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Database: UniProt
Entry: C6VY22_DYAFD
LinkDB: C6VY22_DYAFD
Original site: C6VY22_DYAFD 
ID   C6VY22_DYAFD            Unreviewed;       542 AA.
AC   C6VY22;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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   OrderedLocusNames=Dfer_5735 {ECO:0000313|EMBL:ACT96923.1};
OS   Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS   52180 / NS114).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT96923.1, ECO:0000313|Proteomes:UP000002011};
RN   [1] {ECO:0000313|EMBL:ACT96923.1, ECO:0000313|Proteomes:UP000002011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC   {ECO:0000313|Proteomes:UP000002011};
RX   PubMed=21304649; DOI=10.4056/sigs.19262;
RA   Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA   Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL   Stand. Genomic Sci. 1:133-140(2009).
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; CP001619; ACT96923.1; -; Genomic_DNA.
DR   RefSeq; WP_015815163.1; NC_013037.1.
DR   AlphaFoldDB; C6VY22; -.
DR   STRING; 471854.Dfer_5735; -.
DR   KEGG; dfe:Dfer_5735; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_10; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000002011; 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   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|HAMAP-Rule:MF_01518, ECO:0000313|EMBL:ACT96923.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002011}.
FT   DOMAIN          40..320
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          369..536
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   542 AA;  58983 MW;  510A979483DF3977 CRC64;
     MKANLINIFE KTIQEAEIRI AEKRIAQIDI LGPEDPSLPY ILPGFTDAHV HVESSMLTPA
     QFARLAVVHG TIATVSDPHE IANVLGVEGV HFMIADGKRV PFKFCFGAPS CVPATVFETA
     GAVVDAEQVG ELLASDDIGY LAEVMNFPGV LNKDPDMMAK IHWAKHYNKV IDGHAPGLRG
     DAARRYASFG ISTDHECFTY EEAREKIGYG VKILIREGSA ARNFDALIPL IDEFPDHIMF
     CSDDKHPDNL VEGHINALIK RALASGYNFW NVLQAACINP VLHYSLNAGL LREGDAADFV
     IIDNVYASNI LETWIDGELV AKEGKSLIPD LRSEHPNHFE CALKSPSDFT FSAKNSETRI
     RVIEALDGQL VTNEWLTEAK ITGNAIVPDV ENDVLKVTVV NRYSDAPPSI AFIRNFGLTQ
     GALASSVAHD SHNIICIGCD DASIAQAVNL VIEAGGGLSA VGAGERHVIG LPIAGLMTDR
     DGYEVAKSYT QLDRFVKDQL GSTLKSPFMS LSFMALLVIP SLKLSDKGLF DGENFKFIPL
     TL
//
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