ID B9L5N1_NAUPA Unreviewed; 354 AA.
AC B9L5N1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
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 OrderedLocusNames=NAMH_1275 {ECO:0000313|EMBL:ACM93049.1};
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93049.1, ECO:0000313|Proteomes:UP000000448};
RN [1] {ECO:0000313|EMBL:ACM93049.1, ECO:0000313|Proteomes:UP000000448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC {ECO:0000313|Proteomes:UP000000448};
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM93049.1; -; Genomic_DNA.
DR RefSeq; WP_015902101.1; NC_012115.1.
DR AlphaFoldDB; B9L5N1; -.
DR STRING; 598659.NAMH_1275; -.
DR KEGG; nam:NAMH_1275; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_1_0_7; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000000448; 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; 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; SFLDS00029; Radical_SAM; 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 46..279
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 60
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 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 67
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 354 AA; 40006 MW; 3E7A2BB3F86F83AC CRC64;
MDKLIQKLEN NIEFTLDEAN KLYDLDLSVL GKAAQKIRLD KFGKKTYFNI NRHINPSNIC
KDVCKFCAFS AHRKNPNPYT LSVEECVQIA KNAYEKGAKE VHVVSAHNPE VGYEYYMNIV
KSIKQELPDI HVKAFTAAEV NFFSELSGKS HKEVLEDMAN SGVDSMPGGG AEIFDEQIRN
KICKGKVSSD DWLKIHEIWH TMGKKSNVTM LFGHIEDRIH RIDHIMRIKK LQDKTGGFNA
FIPLVYQRKN NYLNVSKFLT GTEILKTIAI SRILLQNIPN IKAYWVTTTL NLSLVAQEYG
ANDIDGTIEK ESINSAAGAA SSNGLNLNDL VELIKDSGFI PVERDSLYNE IKVY
//
