ID A0A0D6MLS4_9PROT Unreviewed; 623 AA.
AC A0A0D6MLS4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=Tasa_019_050 {ECO:0000313|EMBL:GAN54365.1};
OS Tanticharoenia sakaeratensis NBRC 103193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Tanticharoenia.
OX NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN54365.1, ECO:0000313|Proteomes:UP000032679};
RN [1] {ECO:0000313|EMBL:GAN54365.1, ECO:0000313|Proteomes:UP000032679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN54365.1,
RC ECO:0000313|Proteomes:UP000032679};
RA Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL Submitted (OCT-2012) 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};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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:GAN54365.1}.
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DR EMBL; BALE01000019; GAN54365.1; -; Genomic_DNA.
DR RefSeq; WP_048848908.1; NZ_BAQF01000006.1.
DR AlphaFoldDB; A0A0D6MLS4; -.
DR STRING; 1231623.Tasa_019_050; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000032679; Unassembled WGS sequence.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000032679}.
FT DOMAIN 280..376
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 437..566
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 623 AA; 68027 MW; 47AD5DEC33D10932 CRC64;
MTDVLPADLI TTAPDEVAIR QALVQVALGR KPADIAIRVG RLLDVHTRRW LDDQEIVISN
RRIAWVGAAG TYPGEVRMRE ARPHLAAVPG FGEVHKHIES SHLTPEYEAA LVLPRGNTWT
CEASHEMSNV DGPNNLAFWL AARQNGSPLK IFPLPGSAVP PTGYERGGGY FGLDEQRAFL
KTNLMVAGLD EVMDWPSVSD PASPSYDRLW GMIQATFEQR GVVEGHGAGL REPSVVNAFA
AAGLASDHEV RTPEEMFRKL AAGVFVEIRP VSIPTLVPAL LEAGLADFSQ IALTTDDRSA
SDTLRLGASD YNVRLAIEAG VAPEVAIQCV TINPARHMRL TPWVGSISPG RFADFVLLSD
VATLQIAEVW ADGKQVSQGT TYTGPLPKID WPDWARRTIN VGRDLTAQDF EIPAASGRAT
MNAAVLRPFH WTDDFLTETL AVEDGLVQRD SDRCITKFAI VDRYSGKAQV ARMFWRGCGP
RTPDTALACS VAHDQHNIWV VGSSDAAMAQ AVNAIAAQQG GWALVREGEV AATVRYEIGG
LMSARTAEEL DAEMQDLYAA AEEVDWMHEP TYVDGWPEGF PERLIFATLT CAPWRWVLVA
PHPERAPEGF VNVQTGKTHP IVW
//
