ADEC_FLAPJ
ID ADEC_FLAPJ Reviewed; 540 AA.
AC A6GYI0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=FP1059;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL43153.1; -; Genomic_DNA.
DR RefSeq; WP_011963204.1; NC_009613.3.
DR RefSeq; YP_001295964.1; NC_009613.3.
DR AlphaFoldDB; A6GYI0; -.
DR SMR; A6GYI0; -.
DR STRING; 402612.FP1059; -.
DR EnsemblBacteria; CAL43153; CAL43153; FP1059.
DR GeneID; 66552457; -.
DR KEGG; fps:FP1059; -.
DR PATRIC; fig|402612.5.peg.1073; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_10; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000006394; 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 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; Reference proteome.
FT CHAIN 1..540
FT /note="Adenine deaminase"
FT /id="PRO_0000300158"
SQ SEQUENCE 540 AA; 59529 MW; 768C691DA098CF86 CRC64;
MQIQGQIVDI ENKRIYSGEI TIQNGKIISI IEKNHEVKNY ILPGFIDAHI HIESSMLVPS
EFAKIAVLHG TVATISDPHE IANVLGKKGV YYMIENGKQV PLKFHFGAPS CVPATAFETA
GAIIDSEEIK ELMASPDIYY LSEMMNYPGV LFDDDEVLKK IAWAKHFNKP IDGHAPGLRG
EPIKKYISAG ITTDHECFTY SEAQEKLSLG MKVIIREGSA AKNFEALIDL LPANYENMMF
CSDDKHPDDL ILGHINLLCA RAVAKGIDVF KILQVACVNP VHHYKMKVGL LKKNDAADFI
VVEDLVNFKV NKTYINGELV AENGQSFVEN INFETPNNFN ITKKKISDFE IPSLAEKIRV
IEALEGQLIT NEIHHNSFIK NGKLVSDIEN DILKMAVVNR YQNTTPAIAF IKNFGLKKGA
IASSVAHDCH NIVVVGTSDE EICNAVNLII KNTGGICAVN GTQNKSLALP VAGIMSDKDA
WETGKLYQEI DAMAKDLGST LKAPFMTLSF MALLVIPDLK LSDKGLFSGN TFSFVDLNVE