MQNE_STRCO
ID MQNE_STRCO Reviewed; 387 AA.
AC Q8CJT5;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Aminodeoxyfutalosine synthase {ECO:0000255|HAMAP-Rule:MF_00993};
DE Short=AFL synthase {ECO:0000255|HAMAP-Rule:MF_00993};
DE Short=Aminofutalosine synthase {ECO:0000255|HAMAP-Rule:MF_00993};
DE EC=2.5.1.120 {ECO:0000255|HAMAP-Rule:MF_00993};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnE {ECO:0000255|HAMAP-Rule:MF_00993};
GN Name=mqnE {ECO:0000255|HAMAP-Rule:MF_00993}; OrderedLocusNames=SCO4494;
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).
CC -!- FUNCTION: Radical SAM enzyme that catalyzes the addition of the
CC adenosyl radical to the double bond of 3-[(1-carboxyvinyl)oxy]benzoate,
CC leading to aminodeoxyfutalosine (AFL), a key intermediate in the
CC formation of menaquinone (MK, vitamin K2) from chorismate.
CC {ECO:0000255|HAMAP-Rule:MF_00993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-[(1-carboxyvinyl)-oxy]benzoate + H2O + S-adenosyl-L-
CC methionine = 6-amino-6-deoxyfutalosine + H(+) + hydrogencarbonate +
CC L-methionine; Xref=Rhea:RHEA:33075, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64286, ChEBI:CHEBI:76981;
CC EC=2.5.1.120; Evidence={ECO:0000255|HAMAP-Rule:MF_00993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00993};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_00993};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00993}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnE family.
CC {ECO:0000255|HAMAP-Rule:MF_00993}.
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DR EMBL; AL939120; CAD55486.1; -; Genomic_DNA.
DR RefSeq; NP_733640.1; NC_003888.3.
DR RefSeq; WP_003974455.1; NZ_VNID01000017.1.
DR AlphaFoldDB; Q8CJT5; -.
DR SMR; Q8CJT5; -.
DR STRING; 100226.SCO4494; -.
DR GeneID; 1099934; -.
DR KEGG; sco:SCO4494; -.
DR PATRIC; fig|100226.15.peg.4564; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_0_0_11; -.
DR InParanoid; Q8CJT5; -.
DR OMA; HIKAYWA; -.
DR PhylomeDB; Q8CJT5; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IBA:GO_Central.
DR GO; GO:0102573; F:aminodeoxyfutalosine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00993; MqnE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR022432; MqnE.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03700; mena_SCO4494; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..387
FT /note="Aminodeoxyfutalosine synthase"
FT /id="PRO_0000425130"
FT DOMAIN 52..279
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00993"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00993"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00993"
SQ SEQUENCE 387 AA; 44420 MW; D842730E90A97C4F CRC64;
MDAGLKRELE QKVRSGERLT REDGIALYES DDLAWLGGLA HEVRTRKNGD VVHFNVNRHL
NMTNVCTASC AYCSFQRKPG EKDAYTMRIE EAVKLAKAME GENLTELHIV NGLHPNLPWR
YYPRSLRELK AALPEVSLKA FTATEIHHFE TISGMSASDI LDELIDAGLE SLTGGGAEIF
DWEVRQHIVD HRTHWEDWSR IHRLAHEKGL KTPCTMLYGH IEEPRHRVDH VLRLRELQDE
TGGFQVFIPL RYQHDFVDMK DGKVRNRLQA RTQMATGAEA LKTFAVSRLL FDNVPHVKVF
WVMHGVQTAQ LALQHGADDM DGSVVEYKIT HDADDFGTPN KLTREDLLDL IRDAGFRPVE
RNTRYEILRE YEGPDPARRE SPQPMRV
