ID R5KSJ5_9FIRM Unreviewed; 572 AA.
AC R5KSJ5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=BN508_00344 {ECO:0000313|EMBL:CCY69808.1};
OS Eubacterium sp. CAG:161.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262881 {ECO:0000313|EMBL:CCY69808.1, ECO:0000313|Proteomes:UP000018318};
RN [1] {ECO:0000313|EMBL:CCY69808.1, ECO:0000313|Proteomes:UP000018318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:161 {ECO:0000313|Proteomes:UP000018318};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY69808.1}.
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DR EMBL; CAYQ010000083; CCY69808.1; -; Genomic_DNA.
DR AlphaFoldDB; R5KSJ5; -.
DR STRING; 1262881.BN508_00344; -.
DR Proteomes; UP000018318; 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:UP000018318}.
FT DOMAIN 65..348
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 399..568
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 572 AA; 62581 MW; A990CB0C9DC2B2E5 CRC64;
MHDNIKKRIN IAAKRQPADL VIKNCKIVNV FTHEIIEGDI AISDGKIAAV GNYSGEKEVD
AEGRYALPGF INSHIHIESS FVSPEEFSRL VVPHGTTTII ADPHEIVNVC GMDGFDYMVK
AGENAALNIK YMLPSCVPCT PWEHAGAVVD SKAISEVINQ DKVFGMGEFM NTVGVINTDS
EVIEKISLCH QAGKLIDGHS PGLKGDDLSA YVTAGIHTDH ESGSLEELKE RLRNGMYVML
RYGSACRELP MLLKGVNEQN SRRCILCADD LQPVTIFEKG DMDEKLRICV ENGIDPITAV
QMATLNAAEC FHLDDRGAIA PNKKADIVLV DDLEKFKIDK VWIEGNLVAD KGNYLADTKH
IGIQKVAGSV KVKDFSIDKL KMHLESDKAT VIGILPDSVV TKKKVMKINR GEDGDFKFDK
NIDVAKVAVV ERHQMTGNVA TALIEGYGIK TGAIAVTVAH DSHNIIVVGT NNEDMAFAVS
KLIELEGGIV VVDGGEVLES MPLPIAGLMS DKNGEWVRDK LTKIHNIAYD RLKVNPNVEP
TMTLCFMSLP VIPEVKITDI GLFDVVEQKF IK
//
