ID A0A0Q4QQE8_9BACL Unreviewed; 378 AA.
AC A0A0Q4QQE8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cyclic dehypoxanthine futalosine synthase {ECO:0000256|HAMAP-Rule:MF_00992};
DE Short=Cyclic DHFL synthase {ECO:0000256|HAMAP-Rule:MF_00992};
DE EC=1.21.98.1 {ECO:0000256|HAMAP-Rule:MF_00992};
DE AltName: Full=Dehypoxanthine futalosine cyclase {ECO:0000256|HAMAP-Rule:MF_00992};
DE Short=DHFL cyclase {ECO:0000256|HAMAP-Rule:MF_00992};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnC {ECO:0000256|HAMAP-Rule:MF_00992};
GN Name=mqnC {ECO:0000256|HAMAP-Rule:MF_00992};
GN ORFNames=ASF12_15070 {ECO:0000313|EMBL:KQO01163.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO01163.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO01163.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO01163.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO01163.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO01163.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Radical SAM enzyme that catalyzes the cyclization of
CC dehypoxanthine futalosine (DHFL) into cyclic dehypoxanthine futalosine
CC (CDHFL), a step in the biosynthesis of menaquinone (MK, vitamin K2).
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehypoxanthine futalosine + S-adenosyl-L-methionine = 5'-
CC deoxyadenosine + cyclic dehypoxanthinylfutalosinate + H(+) + L-
CC methionine; Xref=Rhea:RHEA:33083, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57844, ChEBI:CHEBI:58864,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64270; EC=1.21.98.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00992};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00992};
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_00992};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnC family.
CC {ECO:0000256|HAMAP-Rule:MF_00992}.
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:KQO01163.1}.
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DR EMBL; LMLV01000030; KQO01163.1; -; Genomic_DNA.
DR RefSeq; WP_056039530.1; NZ_LMLV01000030.1.
DR AlphaFoldDB; A0A0Q4QQE8; -.
DR STRING; 1736234.ASF12_15070; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000051722; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046992; F:oxidoreductase activity, acting on X-H and Y-H to form an X-Y bond; IEA:UniProtKB-UniRule.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
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_00992; MqnC; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR022431; Cyclic_DHFL_synthase_mqnC.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00423; CofH family radical SAM protein; 1.
DR NCBIfam; TIGR03699; menaquin_MqnC; 1.
DR PANTHER; PTHR43076; FO SYNTHASE (COFH); 1.
DR PANTHER; PTHR43076:SF1; LIPOYL SYNTHASE 2; 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 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|HAMAP-Rule:MF_00992};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00992};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00992}; Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00992};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00992}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00992};
KW Reference proteome {ECO:0000313|Proteomes:UP000051722};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00992}.
FT DOMAIN 51..291
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 65
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_00992"
FT BINDING 69
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_00992"
FT BINDING 72
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_00992"
SQ SEQUENCE 378 AA; 43010 MW; E76A9AA768DDCA28 CRC64;
MATLDQILDK ALRGERISLE ECIIMFESDE IEKMGKVANE IMLRKHPEPV TTFVVGRNVN
YTNVCDVYCR FCAFYRAPGS KEGYVLDNET IMNKIQETID VNGTEILMQG GTNPDLPFTY
YTDLLKEIKQ RFPDITMHSF SPAEIQKMKE VSDGLSLDEV VRQLHEAGLD SLPGGGAEIL
DDRTRRKISR KKGSYTDWID VMKSAHRHGM NTTATMVYGF GETMEERALH LLRIRDVQDE
CKANGYDSEG FTAFISWPFQ PDNTRMPMEK AKPEEYLKIV AVSRIFLDNI DNLQSSWVTM
GPDMGKLSLA YGCNDFGSTM IEENVVSAAG TTHKVNIELI LKLIREAGKV PAQRNTRYEI
LRMYNESDKA EQDFVMQN
//
