ID   MQND_STRCO              Reviewed;         282 AA.
AC   Q9KXN1; B5MG06;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=1,4-dihydroxy-6-naphtoate synthase {ECO:0000255|HAMAP-Rule:MF_00996};
DE            EC=4.1.-.- {ECO:0000255|HAMAP-Rule:MF_00996};
DE   AltName: Full=Menaquinone biosynthetic enzyme MqnD {ECO:0000255|HAMAP-Rule:MF_00996};
GN   Name=mqnD {ECO:0000255|HAMAP-Rule:MF_00996}; OrderedLocusNames=SCO4326;
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: Catalyzes the conversion of cyclic dehypoxanthine futalosine
CC       (cyclic DHFL) into 1,4-dihydroxy-6-naphthoate, a step in the
CC       biosynthesis of menaquinone (MK, vitamin K2).
CC       {ECO:0000305|PubMed:18801996}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00996, ECO:0000269|PubMed:18801996}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene require menaquinone-4 (MK
CC       4) for their growth, and accumulate cyclic DHFL.
CC       {ECO:0000269|PubMed:18801996}.
CC   -!- SIMILARITY: Belongs to the MqnA/MqnD family. MqnD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00996}.
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DR   EMBL; AB447891; BAG71677.1; -; Genomic_DNA.
DR   EMBL; AL939119; CAB93400.1; -; Genomic_DNA.
DR   RefSeq; NP_628497.1; NC_003888.3.
DR   RefSeq; WP_003974649.1; NZ_VNID01000026.1.
DR   AlphaFoldDB; Q9KXN1; -.
DR   SMR; Q9KXN1; -.
DR   STRING; 100226.SCO4326; -.
DR   GeneID; 1099766; -.
DR   KEGG; sco:SCO4326; -.
DR   PATRIC; fig|100226.15.peg.4395; -.
DR   eggNOG; COG2107; Bacteria.
DR   HOGENOM; CLU_070326_0_0_11; -.
DR   InParanoid; Q9KXN1; -.
DR   OMA; RGCGPLV; -.
DR   PhylomeDB; Q9KXN1; -.
DR   BioCyc; MetaCyc:MON-14867; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00996; MqnD; 1.
DR   InterPro; IPR003773; Menaquinone_biosynth.
DR   InterPro; IPR030869; MqnD.
DR   PANTHER; PTHR37167; PTHR37167; 1.
DR   Pfam; PF02621; VitK2_biosynth; 1.
PE   3: Inferred from homology;
KW   Lyase; Menaquinone biosynthesis; Reference proteome.
FT   CHAIN           1..282
FT                   /note="1,4-dihydroxy-6-naphtoate synthase"
FT                   /id="PRO_0000425127"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00996"
FT   BINDING         57..59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00996"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00996"
SQ   SEQUENCE   282 AA;  30054 MW;  99DAB54228CBC749 CRC64;
     MSADTLQIAY SPCPNDTFVF DALAHGRVPG APALDVTFAD IDITNGMAER GELDVLKVSY
     AVLPYVLDDW ALLPCGGALG RGCGPLVLTR EADADLRGRT VAVPSETSTA YLLFRLWAAD
     TVPGGVGEIV VMPFHEIMPA VRDGKVDAGL VIHEARFTYQ NYGLHKLADM GEHWEHTTGL
     PIPLGAIIAR RSLGAPALTR LADAVRASVR AAWDDPEASR PYVMEHAQEM DPAVADQHIG
     LYVNEFTADL GEDGYAAIRG LLTRAAAEGL VPALGPDALA FP