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Database: UniProt
Entry: C6J7D8_9BACL
LinkDB: C6J7D8_9BACL
Original site: C6J7D8_9BACL 
ID   C6J7D8_9BACL            Unreviewed;       378 AA.
AC   C6J7D8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=POTG_04315 {ECO:0000313|EMBL:EES71087.1};
OS   Paenibacillus sp. oral taxon 786 str. D14.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71087.1, ECO:0000313|Proteomes:UP000003981};
RN   [1] {ECO:0000313|EMBL:EES71087.1, ECO:0000313|Proteomes:UP000003981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D14 {ECO:0000313|EMBL:EES71087.1,
RC   ECO:0000313|Proteomes:UP000003981};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Paenibacillus sp. D14.";
RL   Submitted (MAR-2009) 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; GG696001; EES71087.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6J7D8; -.
DR   eggNOG; COG1060; Bacteria.
DR   HOGENOM; CLU_040406_1_0_9; -.
DR   OrthoDB; 9802027at2; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000003981; 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; SFLDG01064; F420__menaquinone_cofactor_bio; 1.
DR   SFLD; SFLDG01389; menaquinone_synthsis_involved; 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_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:UP000003981};
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;  42655 MW;  6C8C77DE100D5358 CRC64;
     MTAIDDILNK ALQGGRLDLE DTIRLFESDE VEKIGHTANI LMERKHPEPI TTFVIGRNIN
     YTNICDVYCR FCAFYRRPGS EEGYVLPDEV IFQKIQETVD VGGTEILMQG GTNPNLPFSY
     YTNLLKAIKE RFPNITMHSF SPAEIMKMKE VSDGLSLEEV LREIHAAGLD SLPGGGAEIL
     DDRTRRKISR LKGSWRDWMD VMQTAHKIGM NTTATMVIGF GESMEERALH LLRVREAQDE
     CIQNGYPSEG FLAFIPWTFQ PDNTNLKAER QTPEAYLKTV AISRIVLDNI KNLQSSWVTM
     GPEVGKLSLQ YGCNDFGSTM IEENVVSSAG ATHKVNIESI LSIIRSAGKV PAQRNTKYEI
     LRVFDEEATV ERDFIMQN
//
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