ID ADEC1_OENOB Reviewed; 553 AA.
AC Q04HC1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Adenine deaminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade1 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=OEOE_0158;
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
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DR EMBL; CP000411; ABJ56151.1; -; Genomic_DNA.
DR RefSeq; WP_002818073.1; NC_008528.1.
DR AlphaFoldDB; Q04HC1; -.
DR SMR; Q04HC1; -.
DR STRING; 203123.OEOE_0158; -.
DR GeneID; 75064983; -.
DR KEGG; ooe:OEOE_0158; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR Proteomes; UP000000774; 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; Manganese; Reference proteome.
FT CHAIN 1..553
FT /note="Adenine deaminase 1"
FT /id="PRO_0000292389"
SQ SEQUENCE 553 AA; 60871 MW; C1F7C92271147EF0 CRC64;
MGKQVYLHIF NAKILDVFNQ RFEDTELWID NGSIYFRGKS KDLTAKNNFN AEGNYIVPGL
IDAHLHIESS LLAPSELAKL ELRHGVTSIF ADPHEIGSVS GVSGLFYMIQ EARNTPLHIH
YMLPSSVPAT NFEHAGAVLH ADALKPFYGF PEINGLAEVM DFPAVANGDP DMLEKIRDAQ
AAGHHADGHG AGLTREQLAV YRAVGIDTDH ESTSGKEALE RIQAGMKVFI REGTVERDEK
SILPVVRKNN QSYFSFCTDD KSAIDIQKEG SVDNNVRLAI SKGIPAERAF TMASYNAAVA
QHVKNVGALT DGFIADLVII SNLDNFVTEK VMTEGNWVDK LESKVTTFTS PAVNAELSLN
DLKLPLKSDK AHVINIQPEH ITTKHTIESV NRDQQGNFVA DQDYAKIIVA ERYHNLGHGL
GIIHGFNMQE GAIGSTIAHD SHNMIIAGVD DKPMIIAYDR LKRMGGGMIL VDKNGFTREL
PLEIAGLMSD KPYQEVIAKQ KSLKGAFAKI SKGIDFDPFL TLSFMALPVI PSLKITDQGL
FDFDQFKFID INA
//
