GenomeNet

Database: UniProt
Entry: A0A075KB62_9FIRM
LinkDB: A0A075KB62_9FIRM
Original site: A0A075KB62_9FIRM 
ID   A0A075KB62_9FIRM        Unreviewed;       570 AA.
AC   A0A075KB62;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=UFO1_1839 {ECO:0000313|EMBL:AIF51390.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF51390.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF51390.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF51390.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP008852; AIF51390.1; -; Genomic_DNA.
DR   RefSeq; WP_038670175.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075KB62; -.
DR   STRING; 484770.UFO1_1839; -.
DR   KEGG; puf:UFO1_1839; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000027983; 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   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:UP000027983}.
FT   DOMAIN          64..336
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          395..563
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   570 AA;  61501 MW;  1F0F45BDAD5786A7 CRC64;
     MKPIEQLISV AQGHVPADVV LKNAQVFNVF TGKFDRGDVA VVGGYIAGIG QYEGQIEIDM
     TGKFITPGFI DGHVHMESSM VSPREFAKVV VTMGTTTLIV DPHEIANVVG EQGIEYVLDV
     AEELPVHIFI MLPSCVPATN LETSGANLTV QELARFINHS RVLGLGELMD FPGVLRRDKD
     TLAKIRLAEG KLIDGHGPEL SGNKLTAYIA AGIGSDHECV TPEEAIERVR QGMYIMLREG
     SAAKNLLNLL PMVNGYTARR CMFATDDRHP ADLINQGHIN HMVKMSIDAG IDLATVLQIA
     TINPATYFNL KDIGAIAPGY YADLLVFDDL ISWVPTLVYK EGQIVATKGK SVFNVLKMND
     KKICNTMHLG NISPVQLKIK ASSRVARVIG LIPHQLITAS LVIEVPVING EFVPDRDNDI
     LKLAVFERHH GTGNVGVGLV KGLGMSAGAI ASTVAHDSHN VVVIGSDDDD MIMAVQEVEK
     MHGGIAIVNE GKVLGTLALP LAGLMSEEDL YTVHIKLTDL HNIARGLGVN PNYDPFMTLA
     FMSLPVIPSL KLTDKGLVDV NKFAVVPVSI
//
DBGET integrated database retrieval system