ID A0A099XPN3_9FLAO Unreviewed; 540 AA.
AC A0A099XPN3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=PHEL85_3193 {ECO:0000313|EMBL:KGL58921.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL58921.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL58921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL58921.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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:KGL58921.1}.
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DR EMBL; JPDS01000003; KGL58921.1; -; Genomic_DNA.
DR RefSeq; WP_036827379.1; NZ_JPDS01000003.1.
DR AlphaFoldDB; A0A099XPN3; -.
DR STRING; 1250005.PHEL85_3193; -.
DR eggNOG; COG1001; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000029991; 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, ECO:0000313|EMBL:KGL58921.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 40..320
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 368..533
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 540 AA; 59144 MW; 0898C7890954A207 CRC64;
MIVQGNIVDI QNKRIFKGEI EVINGKISSI KEENHNQENY ILPGFIDAHI HIESSMLVPS
EFAKIALKHG TVATVSDPHE IANVLGVKGV EFMIENGKKV PLKFNFGAPS CVPATSFESA
GAIIDADDIK LMMENPDIKY LAEMMNYPGV LFDDAEVLAK IQHAKNNNKP IDGHAPGLRG
DDVTKYISAG ISTDHECFSY DEALEKLQKG MKVIIREGSA AKNFEALINL LPEYFENMMF
CSDDKHPDDL LLGHINQVCG RAVAKGIDVF KVLQAACVNP VKHYGLDVGL LQKGDFADFV
LVDSLEKFNV LETYINGELV AKNGESFVKS VDFEVLNNFD TDKKKVVDFR FDSNVEKIRV
IEALDGELVT NQIEANSLIV DGNLVSNTET DVLKMTVVNR YKNDEPAIAF IKNFGIKEGA
IASSVGHDSH NIIAVGVSDE AICKAVNLII ENRGGVCAVN ATEEKIVSLP VAGIMSDKSA
EEIGKAYAEL DKMAKEMGSK LRAPYMSLSF MALLVIPSLK LSDKGLFDGT SFQFTSLEIE
//
