MQND_THET8
ID MQND_THET8 Reviewed; 272 AA.
AC Q5SI12;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=TTHA1568;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP TARTARATE, ACTIVE SITE, AND REACTION MECHANISM.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=19602440; DOI=10.1016/j.jsb.2009.07.007;
RA Arai R., Murayama K., Uchikubo-Kamo T., Nishimoto M., Toyama M.,
RA Kuramitsu S., Terada T., Shirouzu M., Yokoyama S.;
RT "Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme
RT from Thermus thermophilus HB8.";
RL J. Struct. Biol. 168:575-581(2009).
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). {ECO:0000255|HAMAP-
CC Rule:MF_00996, ECO:0000269|PubMed:18801996}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00996, ECO:0000269|PubMed:18801996}.
CC -!- MISCELLANEOUS: The tartarate seen in the active site in the
CC crystallographic structure may partially mimic the substrate; it is
CC suspected that the tartarate may resemble the open-chain form of the
CC ribose part of the substrate, cyclic dehypoxanthine futalosine.
CC {ECO:0000305|PubMed:19602440}.
CC -!- SIMILARITY: Belongs to the MqnA/MqnD family. MqnD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00996}.
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DR EMBL; AB447893; BAG71679.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71391.1; -; Genomic_DNA.
DR RefSeq; WP_011228771.1; NC_006461.1.
DR RefSeq; YP_144834.1; NC_006461.1.
DR PDB; 2CZL; X-ray; 1.55 A; A=1-272.
DR PDB; 3A3U; X-ray; 1.65 A; A=1-272.
DR PDBsum; 2CZL; -.
DR PDBsum; 3A3U; -.
DR AlphaFoldDB; Q5SI12; -.
DR SMR; Q5SI12; -.
DR STRING; 300852.55772950; -.
DR EnsemblBacteria; BAD71391; BAD71391; BAD71391.
DR GeneID; 3168082; -.
DR KEGG; ttj:TTHA1568; -.
DR PATRIC; fig|300852.9.peg.1539; -.
DR eggNOG; COG2107; Bacteria.
DR HOGENOM; CLU_070326_0_0_0; -.
DR OMA; RGCGPLV; -.
DR PhylomeDB; Q5SI12; -.
DR UniPathway; UPA00079; -.
DR EvolutionaryTrace; Q5SI12; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..272
FT /note="1,4-dihydroxy-6-naphtoate synthase"
FT /id="PRO_0000425126"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19602440"
FT BINDING 55..57
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2CZL"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2CZL"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:2CZL"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:2CZL"
SQ SEQUENCE 272 AA; 30034 MW; 08CAC9E13BB9BA20 CRC64;
MEALRLGFSP CPNDTFIFYA LVHGRVESPV PLEPVLEDVE TLNRWALEGR LPLTKLSYAA
YAQVRDRYVA LRSGGALGRG VGPLVVARGP LQALEGLRVA VPGRHTTAYF LLSLYAQGFV
PVEVRYDRIL PMVAQGEVEA GLIIHESRFT YPRYGLVQVV DLGAWWEERT GLPLPLGAIL
ARRDLGEGLI RALDEAVRRS VAYALAHPEE ALDYMRAHAQ ELSDEVIWAH VHTYVNAFSL
DVGEEGERAV ARLFAEAEAR GLAAPSPRPL FV
