ID A0A1C0ZRG5_9BACL Unreviewed; 378 AA.
AC A0A1C0ZRG5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=A8709_22685 {ECO:0000313|EMBL:OCT10650.1};
OS Paenibacillus pectinilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT10650.1, ECO:0000313|Proteomes:UP000093309};
RN [1] {ECO:0000313|Proteomes:UP000093309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-2016) 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:OCT10650.1}.
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DR EMBL; LYPC01000030; OCT10650.1; -; Genomic_DNA.
DR RefSeq; WP_065859078.1; NZ_LYPC01000030.1.
DR AlphaFoldDB; A0A1C0ZRG5; -.
DR STRING; 512399.A8709_22685; -.
DR OrthoDB; 9802027at2; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000093309; 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; SFLDF00342; cyclic_dehypoxanthine_futalosi; 1.
DR SFLD; SFLDG01064; F420__menaquinone_cofactor_bio; 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:UP000093309};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00992}.
FT DOMAIN 51..288
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; 42918 MW; AAD8CA151562EB0F CRC64;
MKPIDRILNK AQAGGRIDVE ECITLFESDQ IEKIGDTANQ IMKKWHPDPI TTFVIGRNIN
YTNICDVYCR FCAFYRPPGS KEGYVLPDET IFQKIQETLD VDGTEILMQG GTNPNLPFSY
YTNILREIKK RFDITMHSFS PAEIMKMKDV SDGLSLEEVV RQLHEAGLDS LPGGGAEILD
DRTRRKISKL KGSWRDWMDV MQTAHKIGMH TTGTMVIGFG ESMEERALHM LRIRDAQDDV
LLQKLNTPGF LAFIPWTFQP DNTNMKAEKV TPEEYLKTLA ISRIMLDNVP NFQSSWVTMG
PEVGKQTLSY GCNDFGSTMI EENVVSAAGT THKVNVSSTL DIIRQAGKIP AQRNTKYQIL
RVFDDENVKI DRDFVMQN
//
