MQNC_STRCO
ID MQNC_STRCO Reviewed; 399 AA.
AC Q9XAP2; B5MG05;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cyclic dehypoxanthine futalosine synthase {ECO:0000255|HAMAP-Rule:MF_00992};
DE Short=Cyclic DHFL synthase {ECO:0000255|HAMAP-Rule:MF_00992};
DE EC=1.21.98.1 {ECO:0000255|HAMAP-Rule:MF_00992};
DE AltName: Full=Dehypoxanthine futalosine cyclase {ECO:0000255|HAMAP-Rule:MF_00992};
DE Short=DHFL cyclase {ECO:0000255|HAMAP-Rule:MF_00992};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnC {ECO:0000255|HAMAP-Rule:MF_00992};
GN Name=mqnC {ECO:0000255|HAMAP-Rule:MF_00992}; OrderedLocusNames=SCO4550;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ROLE IN MENAQUINONE
RP BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=18801996; DOI=10.1126/science.1160446;
RA Hiratsuka T., Furihata K., Ishikawa J., Yamashita H., Itoh N., Seto H.,
RA Dairi T.;
RT "An alternative menaquinone biosynthetic pathway operating in
RT microorganisms.";
RL Science 321:1670-1673(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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:0000305|PubMed:18801996}.
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:0000255|HAMAP-Rule:MF_00992};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00992};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00992, ECO:0000269|PubMed:18801996}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene require menaquinone-4 (MK
CC 4) for their growth, and accumulate a small amount of DHFL.
CC {ECO:0000269|PubMed:18801996}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MqnC family.
CC {ECO:0000255|HAMAP-Rule:MF_00992}.
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DR EMBL; AB447890; BAG71676.1; -; Genomic_DNA.
DR EMBL; AL939120; CAB44543.1; -; Genomic_DNA.
DR PIR; T34636; T34636.
DR RefSeq; NP_628712.1; NC_003888.3.
DR RefSeq; WP_011029726.1; NZ_VNID01000017.1.
DR AlphaFoldDB; Q9XAP2; -.
DR SMR; Q9XAP2; -.
DR STRING; 100226.SCO4550; -.
DR GeneID; 1099990; -.
DR KEGG; sco:SCO4550; -.
DR PATRIC; fig|100226.15.peg.4622; -.
DR eggNOG; COG1060; Bacteria.
DR HOGENOM; CLU_040406_1_0_11; -.
DR InParanoid; Q9XAP2; -.
DR OMA; ATMMFGS; -.
DR PhylomeDB; Q9XAP2; -.
DR BioCyc; MetaCyc:MON-14865; -.
DR BRENDA; 1.21.98.1; 5998.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IBA:GO_Central.
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:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 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/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR020050; FO_synthase_su2.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03699; menaquin_MqnC; 1.
DR TIGRFAMs; TIGR00423; TIGR00423; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Menaquinone biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..399
FT /note="Cyclic dehypoxanthine futalosine synthase"
FT /id="PRO_0000425128"
FT DOMAIN 56..288
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00992"
SQ SEQUENCE 399 AA; 44221 MW; C0A977221DAB0A3C CRC64;
MTEKADLQPI LDRAAAGGRI TPEEALDLYR DAPLHALGAA ADAVRRRRYA GTEHIATYII
ERNINYTNVC VTACKFCAFY AAPKDTKKGW SRDLDDILRR CAETVELGGT QIMFQGGHHP
DYGVEYYEEH FAAIKKEFPQ LVIHSLGASE VEHMARISKV SVEEAIRRIH AAGLDSFAGA
GAELLPERPR KAIAPLKESG ERWLEIMEIA HGLGVESTST MLMGTGETNA ERIEHLRMIR
DVQDRTGGFR AFIPYTYQPE NNHLKGRTQA TLFEYLRMIA IARVFLDNVA HIQGSWLTTG
KEVGQLSLHY GADDLGSIML EENVVSSAGA KHRSNRLEII DLIRKAGRVP AQRATTYEHL
VVHDDPANDP VDERVVSHIS STAIEGGTAH PELKLLAPN
