MQNE_THET8
ID MQNE_THET8 Reviewed; 372 AA.
AC Q5SK48;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=TTHA0804;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, GENE NAME, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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: 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, ECO:0000269|PubMed:24083939}.
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 ECO:0000269|PubMed:24083939};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:24083939};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is likely coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:24083939};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00993, ECO:0000269|PubMed:24083939}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnE family.
CC {ECO:0000255|HAMAP-Rule:MF_00993}.
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DR EMBL; AP008226; BAD70627.1; -; Genomic_DNA.
DR RefSeq; WP_011172898.1; NC_006461.1.
DR RefSeq; YP_144070.1; NC_006461.1.
DR AlphaFoldDB; Q5SK48; -.
DR SMR; Q5SK48; -.
DR STRING; 300852.55772186; -.
DR BindingDB; Q5SK48; -.
DR ChEMBL; CHEMBL4523327; -.
DR EnsemblBacteria; BAD70627; BAD70627; BAD70627.
DR GeneID; 3169961; -.
DR KEGG; ttj:TTHA0804; -.
DR PATRIC; fig|300852.9.peg.798; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_0_0_0; -.
DR OMA; HIKAYWA; -.
DR PhylomeDB; Q5SK48; -.
DR BioCyc; MetaCyc:MON-18457; -.
DR BRENDA; 2.5.1.120; 2305.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..372
FT /note="Aminodeoxyfutalosine synthase"
FT /id="PRO_0000425129"
FT DOMAIN 53..292
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 69
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"
FT BINDING 76
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 372 AA; 42613 MW; DD5EE236FBBF7195 CRC64;
MRGIRDPRLI PIAEKVMEGK RLSFEDGLVL YQTKDLPTLM RLANLVRERK HGHKTYFVHS
IRVSQTNICY VGCTFCAFQR RFGEEGAWDW DVDEVVAWVK ERYQPGLTEI HLTAGHHPKR
PFAYYLDLVR ALKENFPGVQ VKAWTAAEIH HFSKIARLPY REVLKALKEA GLDAMPGGGA
EIFAERVRRK IARAKVSAEG WLEIHRTAHE LGIPTNATML YGHIETLEER LDHMDRLRRL
QDETGGFMSF IPLAFQPDGN QLARELGKKE FTTGLDDLRN LAVARLYLDN FPHIKGYWAT
LTPELAQVSL DWGVTDVDGT LIEERIVHMA GSPTPQGLTK RELARIILMA GRIPVERDAL
YREVRVWDRV EA
