(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 74.
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}.
DR   EMBL; CP000478; ABK16117.1; -; Genomic_DNA.
DR   SMR; A0LFB5; -.
DR   STRING; 335543.Sfum_0417; -.
DR   EnsemblBacteria; ABK16117; ABK16117; Sfum_0417.
DR   KEGG; sfu:Sfum_0417; -.
DR   eggNOG; ENOG4105CPN; Bacteria.
DR   eggNOG; COG1001; LUCA.
DR   HOGENOM; HOG000276949; -.
DR   KO; K01486; -.
DR   OMA; HEIANVM; -.
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;
DR   PRODOM; A0LFB5.
DR   SWISS-2DPAGE; A0LFB5.
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
//

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