ID A0A2H5WJV2_UNCXX Unreviewed; 369 AA. AC A0A2H5WJV2; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 13-SEP-2023, entry version 16. 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 ECO:0000313|EMBL:GBC89209.1}; GN ORFNames=HRbin13_01347 {ECO:0000313|EMBL:GBC89209.1}; OS bacterium HR13. OC Bacteria. OX NCBI_TaxID=2035408 {ECO:0000313|EMBL:GBC89209.1}; RN [1] {ECO:0000313|Proteomes:UP000236227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Kato S., Suzuki K.; RT "Metaegenomics of thermophilic ammonia-oxidizing enrichment culture."; RL Submitted (SEP-2017) 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:GBC89209.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BEHP01000161; GBC89209.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2H5WJV2; -. DR UniPathway; UPA00079; -. 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; PF13394; Fer4_14; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004762; CHP00423; 1. DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1. DR SFLD; SFLDG01389; menaquinone_synthsis_involved; 1. DR SFLD; SFLDS00029; Radical_SAM; 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|ARBA:ARBA00022485, 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}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00993, ECO:0000313|EMBL:GBC89209.1}. FT DOMAIN 61..289 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT BINDING 75 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 79 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 82 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 369 AA; 41889 MW; 22ACFB5C56107F39 CRC64; MNIAGLVEKV QDKNLRRIGE KVLKGERLSP EDAIYLFYSP ELAYIGALAE YVNRKKNGMF AYFIVNRQIN PTNVCIYQCS FCAFGVTKSD PRAYEMSLED ILKKVGETYA QGGREVHIVG GIPHHWKAED YVRLVREVKR AFPEITLKAW TAIEIHHMSK ISGRSYEDIL KELKDAGVEV LPGGGAEIFS ERVRSIIAPY KANAQEYLEV HRTAHKLGIP TNATMLYGHV ETYEERVEHM LKLRELQDET GGFQVFIPLA YWPEGTKLGG KRTSSVDDLK TIAISRLFLD NFEHIKAYWV TLGEKVAQIA LNFGADDIDG TIEEEKIVHS AGTKSAYGHS RERLIKLIRD AQKIPVERDT FYRPVSIHS //