ID A0A417YHZ6_9BACI Unreviewed; 579 AA.
AC A0A417YHZ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=D1B31_21390 {ECO:0000313|EMBL:RHW32479.1};
OS Neobacillus notoginsengisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1578198 {ECO:0000313|EMBL:RHW32479.1, ECO:0000313|Proteomes:UP000284416};
RN [1] {ECO:0000313|EMBL:RHW32479.1, ECO:0000313|Proteomes:UP000284416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30743 {ECO:0000313|EMBL:RHW32479.1,
RC ECO:0000313|Proteomes:UP000284416};
RX PubMed=28786779; DOI=10.1099/ijsem.0.001975;
RA Zhang M.Y., Cheng J., Cai Y., Zhang T.Y., Wu Y.Y., Manikprabhu D., Li W.J.,
RA Zhang Y.X.;
RT "Bacillus notoginsengisoli sp. nov., a novel bacterium isolated from the
RT rhizosphere of Panax notoginseng.";
RL Int. J. Syst. Evol. Microbiol. 67:2581-2585(2017).
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:RHW32479.1}.
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DR EMBL; QWEG01000019; RHW32479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417YHZ6; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000284416; 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:SF6; ADENINE DEAMINASE YERA-RELATED; 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}.
FT DOMAIN 77..361
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 409..570
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 579 AA; 66318 MW; 446AB128EED67892 CRC64;
MEQRYRWKNK HLREHVDVLD GRLSPTILLK NATYLNQTFR SWMKANIWIY DDRIVYVGEK
LPPNLVNCNT IDCSGQFIVP GYIEPHAHPF QLYNPHSFAA YAAGRGTTTI INDNMSLVLH
LNKKRAFLLM KDLRSIPATM FWWCRFDPQT EILNEEEVFS HSQIKSWLEH DAVLQGGELT
GWPKLLAGDD MMLHWIQEAK RMRKQIEGHF PGASEKTLAK MMLLGADCDH EAMTGEEVYD
RLMQGYTVSL RHSSIRPDLP RLLDDMNRLG ITAYDQLMFT TDGSSSGFYK DGVIDQMIRI
AIEKGIPVID AYNMATINPA KYYNFAHIHG KIATGRVANL NILSSMEEPC PVSVLAKGKW
VKRDGEFIDS FPELNWDDYG LEPLDLDWEL TEGDLQFSMP FGIQMENAVI TKPYSVSIEV
SRNQLSDSHD ECFFMLIDRN GKWRINTILK GFANKLQGMA SSFSNTGDII LIGKSKADIL
HSFNRMKEIG GGIVVSEREK AICEIPLQLG GLMTELPLEE LMKAEEKLYE VLRERGYAYS
DPVYSLLFFS STHLPYIRIT QQGMYDVMNK MILFPSIMR
//
