ADEC_SYNFM
ID ADEC_SYNFM Reviewed; 576 AA.
AC A0LFB5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Sfum_0417;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000478; ABK16117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LFB5; -.
DR SMR; A0LFB5; -.
DR STRING; 335543.Sfum_0417; -.
DR PRIDE; A0LFB5; -.
DR EnsemblBacteria; ABK16117; ABK16117; Sfum_0417.
DR KEGG; sfu:Sfum_0417; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_7; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000001784; 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; 2.30.40.10; -; 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; PTHR11113:SF2; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01178; ade; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..576
FT /note="Adenine deaminase"
FT /id="PRO_0000292401"
SQ SEQUENCE 576 AA; 61529 MW; F8593358977B12E5 CRC64;
MKWDTGRMAR IIEAAQGKRV VDLCIRRCRL VNVLSGSIDT VDLAIHEGFV AGWGSYRAAR
EIDADGMYVC PGFIDGHIHI ESTLLAPAQF CAAAVPQGTA AVVADPHEIA NVLGLSGIRY
FLEASEGLPL DFFFNLPSCV PATPLETSGA ALRAPDLDAL LPHERLIGLA EMMNFPGVLS
GFPDVIDKLL LFQARRIDGH APQLGDLGLN AYVAAGITSD HECTTLEEAR EKLAKGMTVM
IREGGQSRDL AALLPAVDEH TWPRCCFVSD DVHPDGLLRE GHMNVIVNRA MSLGMAPVRA
LSLAALTPAR HFRLDRRGAL APGYHADFSM SPTLNPWQPE RVFKAGVEVA RDGRLLLDLG
NGNGVAAPPS PMHITRLLAE DLVVPAQPGL LRIIGVREGT LLTRKIVLPP KIHEGAAVAD
LDRDILKLAV YNRYVPDRPP AVAFVQGLGL KEGAIATTVA HDSHNLIVAG ASDADILHVV
DAVRKSGGGM AAGRTGAEVD VLALPIAGLM SDQPVERVAE RLEQLQGRAR AAGSGLRNPF
MALSFLALPV IPELKLTDLG LIDVSTFSPV SLFETS
