ID E3EA44_PAEPS Unreviewed; 368 AA.
AC E3EA44;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Aminodeoxyfutalosine synthase {ECO:0000256|HAMAP-Rule:MF_00993};
DE Short=AFL synthase {ECO:0000256|HAMAP-Rule:MF_00993};
DE Short=Aminofutalosine synthase {ECO:0000256|HAMAP-Rule:MF_00993};
DE EC=2.5.1.120 {ECO:0000256|HAMAP-Rule:MF_00993};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnE {ECO:0000256|HAMAP-Rule:MF_00993};
GN Name=mqnE {ECO:0000256|HAMAP-Rule:MF_00993};
GN ORFNames=PPSC2_20480 {ECO:0000313|EMBL:ADO58336.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58336.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO58336.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO58336.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_00993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00993};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00993}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnE family.
CC {ECO:0000256|HAMAP-Rule:MF_00993}.
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DR EMBL; CP002213; ADO58336.1; -; Genomic_DNA.
DR RefSeq; WP_013372907.1; NC_014622.2.
DR AlphaFoldDB; E3EA44; -.
DR STRING; 1406.LK13_07735; -.
DR KEGG; ppm:PPSC2_20480; -.
DR PATRIC; fig|886882.15.peg.4368; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_1_0_9; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000006868; 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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00993; MqnE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR022432; MqnE.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03700; mena_SCO4494; 1.
DR PANTHER; PTHR43076:SF7; AMINODEOXYFUTALOSINE SYNTHASE; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004762; CHP00423; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00993};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00993};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00993}; Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00993};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00993}; Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00993}; Transferase {ECO:0000256|HAMAP-Rule:MF_00993}.
FT DOMAIN 59..292
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00993"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00993"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00993"
SQ SEQUENCE 368 AA; 41947 MW; 01CCE4CB99A594CA CRC64;
MSTLVTPFTD RRMAEIVEKV QNGIRLNLED GIYLYETDDI LTLGQLANEA NLRKNGKKVY
FIENMSLYFT NVCEARCAFC NFRKDQGEEG SYTLSGQEMI DYVEQHIHPG VREFHIVGGH
NNHVPFQYYV DSLKALNEKY PNVTLKAYTA AEIDFFTRIS GLSIKEVLQE LQKAGLQSLT
GGGAEILSDE YRKKMRVTKA NVDRYLEVHR TAHNLGMKTH TTMLYGSVET YQDRIEHMLQ
IRELQDETNG FMVFIPLSMQ PKSKNANIMR RNSAYEDLKT IAISRLMLDN IDHVKAYFIN
IGPQLTQVAL TFGASDVHGT IVREQISHAA GALTPSGLTR KELIWLVKGA GRIPVERDTF
YNEIEVFE
//
