ID A0A0A7LLD6_9BACT Unreviewed; 550 AA.
AC A0A0A7LLD6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=PK28_05085 {ECO:0000313|EMBL:AIZ63218.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ63218.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ63218.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ63218.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP010054; AIZ63218.1; -; Genomic_DNA.
DR RefSeq; WP_044512061.1; NZ_CP010054.1.
DR AlphaFoldDB; A0A0A7LLD6; -.
DR STRING; 1385664.PK28_05085; -.
DR KEGG; hyd:PK28_05085; -.
DR HOGENOM; CLU_027935_0_0_10; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000030789; Chromosome.
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|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000030789}.
FT DOMAIN 48..328
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 377..543
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 550 AA; 58715 MW; 0447D8A11D50D722 CRC64;
MPSEFQLTAN VVDLFANTIL PGTISVVDGR IQSITPTGAT APDATLPYAL PGFVDAHVHV
ESSLLVPAEF ARLAVVHGTV ATVSDPHEIG NVLGVAGVDY MLASAGHVPF KFCFGAPSCV
PATVFETAGA TITPQDIEQL FQNPKIGYLA EMMNWPGVLH RDAEVMEKIR LAQAYGRPVD
GHAPGLRGED ARQYAAAGIS TDHECFTAEE ALDKLAVGMK ILVREGSAAR NFEALIDLLP
EHHEHMMFCS DDKHPDTLVL GHINQLVQRA VARGQDVRQV LRVACRNPVE HYNLPVGLLR
VGDAADFIVV QNLQDFRVQQ TYLDGVLVAE NGQTRIAPAP CPVVNQFYSQ HLTAADFAVP
TPGDVATVRV MECFDGQLIT ARHDMAATVQ DGYVVADVPQ DVLKLTVVNR YHAAPPAVSF
IQGFGLKQGA LASSVGHDSH NITAVGCDNE SLARAVNLVM EAKGGLAAVG PDGQEMLLPL
PVAGLMSDKD GYHVAEAYAA VDALAKQLGS PLQAPFMTLS FMALLVIPSL KLSDKGLFDG
EAFRFVDAVV
//
