ID A0A0F7N834_9ACTN Unreviewed; 398 AA.
AC A0A0F7N834;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AA958_20560 {ECO:0000313|EMBL:AKH84181.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH84181.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH84181.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH84181.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-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}.
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DR EMBL; CP011492; AKH84181.1; -; Genomic_DNA.
DR RefSeq; WP_047017468.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N834; -.
DR STRING; 444103.AA958_20560; -.
DR KEGG; strc:AA958_20560; -.
DR PATRIC; fig|444103.5.peg.4337; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000034283; Chromosome.
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; 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 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:UP000034283};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00992}.
FT DOMAIN 54..286
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
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_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"
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_00992"
SQ SEQUENCE 398 AA; 43707 MW; 8373385BB70B97AB CRC64;
MTTDLQAVLD RAAAGGRVTP GEALDLYRSA PLHALGAAAD AVRRRRYAGT EHIATYIIER
NINYTNVCVT ACKFCAFYAP PTAKDKGWIR GLDDILRRCE ETVQLGGTQI MFQGGHHPDF
GVEYYEEHFS AIKKAFPQLV IHSLGASEVE HMARISGTTA EDAIRRIHAA GLDSFAGAGA
ELLPARPRQA IAPLKESGER WLEIMESAHG LGVESTSTML MGTGETNAER IEHLRMIRDV
QDRTGGFRAF IPYTYQPENN KLKGRTQATT LEYLRMIAIA RIFLDNVAHI QGSWLTTGKD
VGQLTLHYGA DDLGSVMLEE NVVSSAGARH RSNLREIIEM IRGADRVPAQ RATTYEHLVV
HDDPADDPVD DRVVSHLSST ALDGGTAHPE LTLVEADR
//
