ID A0A0L0QKV3_VIRPA Unreviewed; 582 AA.
AC A0A0L0QKV3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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=AFK71_11665 {ECO:0000313|EMBL:KNE19191.1};
OS Virgibacillus pantothenticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE19191.1, ECO:0000313|Proteomes:UP000036780};
RN [1] {ECO:0000313|Proteomes:UP000036780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10053 dsm26.";
RL Submitted (JUL-2015) 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:KNE19191.1}.
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; LGTO01000007; KNE19191.1; -; Genomic_DNA.
DR RefSeq; WP_050351699.1; NZ_LGTO01000007.1.
DR AlphaFoldDB; A0A0L0QKV3; -.
DR PATRIC; fig|1473.5.peg.878; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000036780; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000036780}.
FT DOMAIN 78..346
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 431..573
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 582 AA; 66073 MW; 19FBD136A300B83A CRC64;
MLRNGFYWRN REMRQHVRVI DGEVAPTIVL KNATYLNTYT KQWLKAVIWI YEDRIVYVGN
QMPANLHNAE IVDCKGKYIV PGYVEPHAHP FQLYNPEQLA LHAAKTGTTT LINDNLLWLF
MLDKKKAFSI LEEFSKHPVS MYWWARFDPQ TELQGEKELD LFQTEDVLAW IKHPAVLQGG
ELTSWPDLLA GDDILLYWIQ ETKNQRKPVE GHFPGASERT LTKMKLLGVN ADHESISGEE
VMRRLRLGYH VGLRHSSIRP DLPKLIEEIL AAGLTTFENV SFTTDGATPS FYEAGLINQC
IEIAIEKGIP VEEAYLMGSY YAAKHLRMEE QLGSIAPGRF AHINILPEKH IPKPESVLAK
GKWIVKGGEQ QKIKPHIQWQ AYQIKPLDLD WELSNKELQF SVPIGLEMAN DVIMTPYPIE
VDITVEELPA ETTDAFLLLL DRNGKWRVNT TLRGFTNQLG AIASSYSVSG DFIFIGKRKS
DILLAGKRLK ELGGGIVIVH QGKVLLEIPL ALGGMMFAGE MDELIGKEKE LKQILQSFGY
PFSDPVYTIF FLSSTHLPYI RITPLGLMDV KKKELLFPAT MC
//
