ID A0A0R2ARQ6_9LACO Unreviewed; 558 AA.
AC A0A0R2ARQ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=FD06_GL001040 {ECO:0000313|EMBL:KRM69552.1};
OS Apilactobacillus ozensis DSM 23829 = JCM 17196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM69552.1, ECO:0000313|Proteomes:UP000052012};
RN [1] {ECO:0000313|EMBL:KRM69552.1, ECO:0000313|Proteomes:UP000052012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM69552.1,
RC ECO:0000313|Proteomes:UP000052012};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM69552.1}.
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DR EMBL; AYYQ01000003; KRM69552.1; -; Genomic_DNA.
DR RefSeq; WP_056965644.1; NZ_AYYQ01000003.1.
DR AlphaFoldDB; A0A0R2ARQ6; -.
DR STRING; 1423781.FD06_GL001040; -.
DR PATRIC; fig|1423781.4.peg.1080; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000052012; 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 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:UP000052012}.
FT DOMAIN 56..338
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 384..551
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 558 AA; 61942 MW; 03ECA43F1CB52334 CRC64;
MMEKVDLCIT NGNVLNVFTR SFEKNTLWIK NGKIVATGNQ FNTIQAKTII NASDKYIVPG
FIDSHVHIES SLVAPSELAK VILPMGTTSI FTDPHEIANV SGVDGIKYMI EDARQTPLDV
FVMLPSSVPC TPFEDNGATL KAKDLHPLYK FPEVKGLAEV MDYPAVEKRD TDIMEKINDA
LNHHLQVDGH GAGMNREQLD VYRQAEISTD HECTDLQGIN DRLAEGFKVF LREGTVERDL
QNTIQIVNEG NAQRFSFCTD DKFINTIIEE GGINFAIKLA IQYGVKPETA YTMASYNAAM
AHKIDDLGAL STGYKADLVF INNPKAVDVN KVMKDGKFIQ ENDFETKTLN FQSNTMNHHF
TKADLKLELS NDECNVIGIC PNHIETKHLI KKVPIENGEF KADLKNDVLK MVDVERHHNS
GTYGLALVSG FKLNEGAVAT TVAHDSHNLL AFGTSDDAIY RAIEEVTKVG GGISVVDDEK
TLATMPLKIA GLMSDKSWQK ASEDLSAITN AYKKISNDID FNPFITLSFL SLPVIPTIKL
TNRGLYDFEQ QKFINIAR
//
