ID   MQNX_STRAW              Reviewed;         358 AA.
AC   Q82K09;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Aminodeoxyfutalosine deaminase;
DE            Short=AFL deaminase;
DE            Short=Aminofutalosine deaminase;
DE            EC=3.5.4.40;
GN   Name=add2; OrderedLocusNames=SAV_2595;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP   MUTAGENESIS OF ARG-87, AND 3D-STRUCTURE MODELING IN COMPLEX WITH AFL.
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=23972005; DOI=10.1021/bi400750a;
RA   Goble A.M., Toro R., Li X., Ornelas A., Fan H., Eswaramoorthy S.,
RA   Patskovsky Y., Hillerich B., Seidel R., Sali A., Shoichet B.K., Almo S.C.,
RA   Swaminathan S., Tanner M.E., Raushel F.M.;
RT   "Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by
RT   distantly related enzymes.";
RL   Biochemistry 52:6525-6536(2013).
CC   -!- FUNCTION: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into
CC       futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin
CC       K2). To a lesser extent, can also deaminate adenosine, 5'-
CC       methylthioadenosine, 5'-deoxyadenosine, and 2'-deoxyadenosine.
CC       {ECO:0000269|PubMed:23972005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+);
CC         Xref=Rhea:RHEA:40075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58863, ChEBI:CHEBI:64286; EC=3.5.4.40;
CC         Evidence={ECO:0000269|PubMed:23972005};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.8 uM for aminodeoxyfutalosine {ECO:0000269|PubMed:23972005};
CC         KM=94 uM for 5'-methylthioadenosine {ECO:0000269|PubMed:23972005};
CC         Note=kcat is 3.8 sec(-1) with aminodeoxyfutalosine as substrate. kcat
CC         is 0.40 sec(-1) with 5'-methylthioadenosine as substrate.;
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
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DR   EMBL; BA000030; BAC70306.1; -; Genomic_DNA.
DR   RefSeq; WP_010984031.1; NZ_JZJK01000064.1.
DR   AlphaFoldDB; Q82K09; -.
DR   SMR; Q82K09; -.
DR   STRING; 227882.SAV_2595; -.
DR   DNASU; 1210477; -.
DR   EnsemblBacteria; BAC70306; BAC70306; SAVERM_2595.
DR   KEGG; sma:SAVERM_2595; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_1_11; -.
DR   OMA; RPQFKPY; -.
DR   OrthoDB; 554648at2; -.
DR   BRENDA; 3.5.4.40; 5980.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01320; ADA; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43114; PTHR43114; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Menaquinone biosynthesis; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..358
FT                   /note="Aminodeoxyfutalosine deaminase"
FT                   /id="PRO_0000425133"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         215
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         87
FT                   /note="R->A: 30-fold reduction in catalytic efficiency with
FT                   AFL as substrate, but nearly no effect on catalytic
FT                   efficiency with adenosine as substrate."
FT                   /evidence="ECO:0000269|PubMed:23972005"
FT   MUTAGEN         87
FT                   /note="R->M: 15-fold reduction in catalytic efficiency with
FT                   AFL as substrate, but nearly no effect on catalytic
FT                   efficiency with adenosine as substrate."
FT                   /evidence="ECO:0000269|PubMed:23972005"
SQ   SEQUENCE   358 AA;  39203 MW;  1E0A507601946B6C CRC64;
     MTEHFDARGT RDAQTGRDLH SFIAGLPKAE LHVHHVGSAS PRIVSELAAR HPDSSVPTDP
     EALADYFTFT DFAHFIKVYL SVVDLIRTPE DVRLLTYEVA RELARQQVRY AELTITPFSS
     TRRGIDERAF MDAIEDARKS AEAEFGTVLR WCFDIPGEAG LESAEETVRL ATDDRLRPEG
     LVSFGLGGPE IGVPRPQFKP YFDRAIAAGL RSVPHAGETT GPETVWDALT DLRAERIGHG
     TSSAQDPKLL AHLAEHRIPL EVCPTSNIAT RAVRTLDEHP VKEFVRAGVV VTINSDDPPM
     FGTDLNNEYA IAARLLDLDE RGLAGLAKNS VEASFLDAAG KARIAAEIDT YTAAWLAP