ID A0A0R1XCD7_9LACO Unreviewed; 567 AA.
AC A0A0R1XCD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=FC91_GL002302 {ECO:0000313|EMBL:KRM27839.1};
OS Schleiferilactobacillus harbinensis DSM 16991.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM27839.1, ECO:0000313|Proteomes:UP000050949};
RN [1] {ECO:0000313|EMBL:KRM27839.1, ECO:0000313|Proteomes:UP000050949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM27839.1,
RC ECO:0000313|Proteomes:UP000050949};
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:KRM27839.1}.
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DR EMBL; AZFW01000040; KRM27839.1; -; Genomic_DNA.
DR RefSeq; WP_027828149.1; NZ_AZFW01000040.1.
DR AlphaFoldDB; A0A0R1XCD7; -.
DR PATRIC; fig|1122147.4.peg.2380; -.
DR eggNOG; COG1001; Bacteria.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000050949; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050949}.
FT DOMAIN 56..339
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 394..559
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 567 AA; 61264 MW; DAEB2ED6A972D41C CRC64;
MTTVDLLLTN GHVFSSALHR FIETDVTVLD GKFYWLPAPG TFTGEAKKTI DLAGTYMIPG
MVDSHMHIES SMTTPTRFGR AVAAHGTTTV IADAHEITNV AGLKGLQEFM AQPSDIDVFY
AIPSSVPSTK PELETTGGII GVAETKELLK DPRIICLGEA MNFKGITSEP DSLIRQLIAE
CRRERPTMPL EGHCPKYTGE DLAKFIYSGI TSDHTQQTPA SILEKVTNGM FVQLQKKSLT
EENIAAVKDH QLFENVALVT DDVMADDLRH GHLNKIVQQA ISLGLDPVDA IYMATYTPAR
HMGLWNRGSI TPGRVADFII LRDLQAFDVV AVYKNGQLVE PAADQSPADP HAFSTDLRHS
VQAKPITAAD LQLRVPDDVS AVTANVIEIA AVGTFTKRVP VKLTVKDHLV QWQDAGLALL
MIQERYGHGG HIAFGLVKGA LSRPGAVGAT WAHDHHNVMV MGTTIADMVA AQNELIAEQG
GYVVAEGGQI VANAPLPIGG VVSDAPIPVL GKQIADVRQA MQDLGYHNTN EIMSFSTLSL
LVSPAFKMSD KGLFDVKSQV KIPLFAE
//
