ID A0A0D7W1Y0_9FLAO Unreviewed; 539 AA.
AC A0A0D7W1Y0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=PK35_09040 {ECO:0000313|EMBL:KJD33096.1};
OS Tamlana nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tamlana.
OX NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD33096.1, ECO:0000313|Proteomes:UP000032361};
RN [1] {ECO:0000313|EMBL:KJD33096.1, ECO:0000313|Proteomes:UP000032361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FHC16 {ECO:0000313|EMBL:KJD33096.1,
RC ECO:0000313|Proteomes:UP000032361};
RX PubMed=25735434; DOI=10.1007/s10482-015-0410-x;
RA Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.;
RT "Tamlana nanhaiensis sp. nov., isolated from surface seawater collected
RT from the South China Sea.";
RL Antonie Van Leeuwenhoek 107:1189-1196(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJD33096.1}.
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DR EMBL; JTDV01000005; KJD33096.1; -; Genomic_DNA.
DR RefSeq; WP_044626373.1; NZ_JTDV01000005.1.
DR AlphaFoldDB; A0A0D7W1Y0; -.
DR STRING; 1382798.PK35_09040; -.
DR PATRIC; fig|1382798.3.peg.3156; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000032361; 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 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 {ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000032361}.
FT DOMAIN 40..320
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 367..532
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 539 AA; 59285 MW; 92DF18B577DD5345 CRC64;
MKVKGQIVDI LNKRIFKGEV TIDNGKIKSI QPKEHHVEQY ILPGFIDAHI HIESSMLVPS
EFAKLAVKHG TVATVSDPHE IANVLGVKGV EFMIENGKQV PFKFNFGAPS CVPATSFESA
GAVINSNDIK KLLENPDIKY LAEMMNYPGV IFEDDEVLKK IAWAKYYNKP VDGHAPGVVG
DDISKYIAAG IYTDHECFTY DEALEKLQKG MRILIREGSA AKNFEALIDL LPDHFENMMF
CSDDKHPDDL LLHHINNLCA RAVAKGTDVF KVLQVACINP VKHYNLDVGL LREGDFADFI
VVEDLKDFKT LQTYVNGELV FNQGESLIAS VDFENLNNFN CSEKDVSAFK IKSEAKQIRV
IEALEGQLVT NEIIEDATVN NGYLESNTEK DILKMAVVNR YNDTEPALAF IKNFGLKKGA
IASSVGHDSH NIIAVGTTDE ALCKAVNLII ENKGGICAVT ASEEKIVPLP VAGIISDQNG
ETIGKQYAEL DAMAKQLGSP LNAPYMTLSF MALLVIPALK LSDKGLFNGK DFKFTSLQA
//
