ID A0A0F3RVQ7_9LACO Unreviewed; 589 AA.
AC A0A0F3RVQ7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=VC81_00455 {ECO:0000313|EMBL:KJW13980.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13980.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW13980.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW13980.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-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, 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 -!- 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:KJW13980.1}.
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DR EMBL; JZCR01000002; KJW13980.1; -; Genomic_DNA.
DR RefSeq; WP_045806178.1; NZ_JZCR01000002.1.
DR AlphaFoldDB; A0A0F3RVQ7; -.
DR STRING; 216463.VC81_00455; -.
DR PATRIC; fig|216463.3.peg.1073; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000033491; Unassembled WGS sequence.
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 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}.
FT DOMAIN 70..357
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 414..577
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 589 AA; 63153 MW; EC4B93B814E74B63 CRC64;
MTTLSHYLDA GAAKLPADLV IENGTLANVD TGEFYPANVA IYRQKIVAVD TDVSAYVGPA
TRHIDATGQY LVPGLIDGHI HVECSKLSMT RFAELVLPHG TTSIVSGLDE YISVVGVAGL
PEIFAEIDAL PFKVFWGLPY KTPYTIPQST IAYNVTAADH AEYLPQDNCY GVWETVREAV
GVRDPDTLKA LELAQRYHKP IFGCSPMARG KALNEFLMSG VHIDHESYSH EEFLEKARKG
LRVVIRESSV TKFLQENIRA ITEGPAGVAR HTSFCTDDVN ARDVLAHGHL DHMVRLAIQA
GVAPMTAIQM ATINGAEAYH VDDRVGSIAP GKAADILLVD QPGTFTVNTV ISQGQVVSHD
HQPALTFTPP HRSATLQGQL KHAPMTADDF RYTVAAATGT ATVRTIHSVG PFVRQARDLD
LPISDHVVLP DPASDVAAVS VIERYGVNQN HARGFLSGWS IKRGAIATSA SPDDNNLVVA
GVDPADMALA ANTLIACGGG QVVVADGQVL TLLKLPIAGI TTDLTPTDLA QKELALKQAA
EQLGSTLPDP LFYLSFLPIT AIPDLAITDG GNVDYTQLTY FDPILKVTH
//
