ID A0A415R6L6_9FIRM Unreviewed; 370 AA.
AC A0A415R6L6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=DWZ54_08380 {ECO:0000313|EMBL:RHM54642.1};
OS Mitsuokella sp. AF33-22.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=2292047 {ECO:0000313|EMBL:RHM54642.1, ECO:0000313|Proteomes:UP000284511};
RN [1] {ECO:0000313|EMBL:RHM54642.1, ECO:0000313|Proteomes:UP000284511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-22 {ECO:0000313|EMBL:RHM54642.1,
RC ECO:0000313|Proteomes:UP000284511};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHM54642.1}.
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DR EMBL; QRQA01000011; RHM54642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415R6L6; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000284511; Unassembled WGS sequence.
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 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; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1.
DR SFLD; SFLDG01389; menaquinone_synthsis_involved; 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};
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 50..287
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 64
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 68
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 71
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 370 AA; 41523 MW; 094FC1924C95B2F3 CRC64;
MADTARARRR AANGERLDLA DAMALYEDND LLFLADCARR AKERKSGRQV FYTVNRHINL
TNICSANCPL CAFQVRAGDA RGYVLERDDI AKILREAQAT KHLSEIHIVS ALHPDKPFSY
YVEVVRQVKE ALPQVDVKAF TPVEIVNFAH MTGKSIREVL IILQEAGLDS LPGGGAEILS
DRVRQIICPK KATAAEWIET MKTAHNLGIR TNASIMYGHV ETIEERLQHL FTIRDIQDET
GGFQAFMLFP FHPAHTELGD TYHLQRTGSW EDMKMMALSR LILDNIDHIK AFWIMLTMPI
AQLALGFGAD DLDGTIGEEK IIHAAGARTN TGITRTKLEA IIRETGYEPV ERDTFYQPVE
AIGKEETSCD
//
