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Database: UniProt
Entry: H1LRP5_9FIRM
LinkDB: H1LRP5_9FIRM
Original site: H1LRP5_9FIRM 
ID   H1LRP5_9FIRM            Unreviewed;       526 AA.
AC   H1LRP5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=HMPREF9099_00122 {ECO:0000313|EMBL:EHO54654.1};
OS   Lachnospiraceae bacterium oral taxon 082 str. F0431.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO54654.1, ECO:0000313|Proteomes:UP000003005};
RN   [1] {ECO:0000313|EMBL:EHO54654.1, ECO:0000313|Proteomes:UP000003005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0431 {ECO:0000313|EMBL:EHO54654.1,
RC   ECO:0000313|Proteomes:UP000003005};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) 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:EHO54654.1}.
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DR   EMBL; AGRL01000003; EHO54654.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1LRP5; -.
DR   PATRIC; fig|861454.3.peg.121; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   Proteomes; UP000003005; 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}.
FT   DOMAIN          67..350
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          402..523
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   526 AA;  57604 MW;  8B4E0367368A991B CRC64;
     MIEKDDLKKL IDVAAGRKKA DLVLKNGNIV DLCGGKILKA DLAIADGLIA GFGEYEGERE
     IDVTGKYISP GLMDAHIHIE SSYTTPEEFG KMVVPHGTTT VIADPHEIVN VCGLKGFSYM
     KNAAENTALD IKYMMPSCVP ATKLEDSGFV ISAEDMKADI VSDDVLGLGE FMDFNAVIQK
     DDTALDKILL AGRHKKIIDG HSPNLKGNSL NAYVCAGINT DHECSTLEEM EDRLSRGIYV
     QLRQGSACHN LKALIPGINE FNFRRCLLCS DDRQPKTIFE EGHLEYHLRT LVRAGISPVM
     ALSMATVNVS DCYRLFDRGI IAPGKRADLV VFDDLYDFPV SSVFILGEEV ARDGKYLRDT
     ERYDISEVSD TVCLNNFKKE MLQMWLKSND VYAIEMIAGG VLSKKSKIRV KRRDGLFVFD
     KDIDACKCAV IERHHNTGKV GLGIIKGYGI KCGAIAASVA HDSHNIICIG TNDDDMYLAI
     ENIKENGGGF ALAKDGKILE SLSLPVAGLM SDLSGEEVAK KLLGLH
//
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