MQNX_STRCO
ID MQNX_STRCO Reviewed; 387 AA.
AC O86737;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Aminodeoxyfutalosine deaminase;
DE Short=AFL deaminase;
DE Short=Aminofutalosine deaminase;
DE EC=3.5.4.40;
GN OrderedLocusNames=SCO5662; ORFNames=SC6A9.05;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=24083939; DOI=10.1021/ja408594p;
RA Mahanta N., Fedoseyenko D., Dairi T., Begley T.P.;
RT "Menaquinone biosynthesis: formation of aminofutalosine requires a unique
RT radical SAM enzyme.";
RL J. Am. Chem. Soc. 135:15318-15321(2013).
CC -!- FUNCTION: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into
CC futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin
CC K2). {ECO:0000269|PubMed:24083939}.
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:24083939};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000269|PubMed:24083939}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; AL939124; CAA19890.1; -; Genomic_DNA.
DR PIR; T35436; T35436.
DR RefSeq; NP_629792.1; NC_003888.3.
DR RefSeq; WP_011030372.1; NZ_VNID01000024.1.
DR AlphaFoldDB; O86737; -.
DR SMR; O86737; -.
DR STRING; 100226.SCO5662; -.
DR GeneID; 1101101; -.
DR KEGG; sco:SCO5662; -.
DR PATRIC; fig|100226.15.peg.5747; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_7_0_11; -.
DR InParanoid; O86737; -.
DR OMA; RPQFKPY; -.
DR PhylomeDB; O86737; -.
DR BRENDA; 3.5.4.40; 5998.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001973; 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..387
FT /note="Aminodeoxyfutalosine deaminase"
FT /id="PRO_0000194387"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 42430 MW; 660F2621C115EA5A CRC64;
MRPAYDDPRT TDQPITRARP PPRAARGRRL GEEPLTEHLV DPDVPRDLHA FIAGLPKAEL
HVHHVGSASP RIVSELAARH ADSKVPTDPE ALVDYFTFTD FAHFIDVYLS VVDLIRTPED
VRLLTYEVAR DMARQQVRYA ELTITPFSST RRGIDEGAFM DAIEDARKAA EAEFGTVLRW
CFDIPGEAGL ESAEETARLA TDDRLRPEGL VSFGLGGPEI GVARPQFKPY FDRAIAAGLH
SVPHAGETTG PQTVWEALID LRAERIGHGT SSAQDPKLLA HLAERRIPLE VCPTSNIATR
AVRTLDEHPI KEFVRAGVPV TINSDDPPMF GTDLNNEYAV AARLLGLDER GLADLAKNGV
EASFLDAPGK ARIADEIDTY TAAWLAS
