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Database: UniProt
Entry: F8E901_FLESM
LinkDB: F8E901_FLESM
Original site: F8E901_FLESM 
ID   F8E901_FLESM            Unreviewed;       539 AA.
AC   F8E901;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=Flexsi_0437 {ECO:0000313|EMBL:AEI14125.1};
OS   Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Flexistipitaceae; Flexistipes.
OX   NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14125.1, ECO:0000313|Proteomes:UP000006621};
RN   [1] {ECO:0000313|EMBL:AEI14125.1, ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX   PubMed=22180813; DOI=10.4056/sigs.2235024;
RA   Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Genome sequence of the moderately thermophilic halophile Flexistipes
RT   sinusarabici strain (MAS10).";
RL   Stand. Genomic Sci. 5:86-96(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002858; AEI14125.1; -; Genomic_DNA.
DR   RefSeq; WP_013885636.1; NC_015672.1.
DR   AlphaFoldDB; F8E901; -.
DR   STRING; 717231.Flexsi_0437; -.
DR   KEGG; fsi:Flexsi_0437; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000006621; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006621}.
FT   DOMAIN          50..332
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          387..536
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   539 AA;  59099 MW;  E2731322592CC180 CRC64;
     MKTLFENVFI PDFDKNVFFK SNVLINNGVI AEITDSKPYA HEYYKGAGLY ITPGFIDCHV
     HTESSHLTPS AFGDVVLKHG TLHVVTDNHE IANVGGMGAV EYFMDEAKHS FCNIKFAVPS
     CVPATPFATS GAQLGIDEIS SLLEKEETVS LGEMMNNPGV IQGEEKFVVS IAKAKALGKV
     INGHAPGLSG EDLLKYVAAG VMDDHESESY HDIKTKLEAG LKIFLREGSA EHTDNKAYEL
     INEYPDDIMF CTDDKSLNHI LRGGHISYNV NKALKLGIPP VNVLKAASRN GLKYYGLDRY
     SEIKPGMYAS FIIADISSKS FEIKDIYIDG KNLSHFSQKN SHTPIPEKLQ NSMNIVNQSE
     IPQMNNEQAC IRVKDGSLIT EHLVDSSKTY DLENDILKLC VFERYGYGNR TSCKINGFNL
     KRGAFASSIA HDCHNIVAVG TSDESILKVV NSVIDNGGGL AVSDDNSLFT LPLEIGGLVT
     SKAPEAVVES LERINEQIAE MGCTLTDPLG TLSFMALEVI PHLKLTDKGL FDVDNFRFL
//
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