MQNA_STRCO
ID MQNA_STRCO Reviewed; 282 AA.
AC Q9L0T8; B5MG03;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Chorismate dehydratase {ECO:0000255|HAMAP-Rule:MF_00995};
DE EC=4.2.1.151 {ECO:0000255|HAMAP-Rule:MF_00995};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnA {ECO:0000255|HAMAP-Rule:MF_00995};
GN Name=mqnA {ECO:0000255|HAMAP-Rule:MF_00995}; OrderedLocusNames=SCO4506;
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], ROLE IN MENAQUINONE BIOSYNTHESIS,
RP 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "The crystal structure of a hypothetical protein SCO4506 (gene ID: Q9L0T8)
RT from Streptomyces coelicolor to 2.04 Angstrom resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dehydration of chorismate into 3-[(1-
CC carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone
CC (MK, vitamin K2). {ECO:0000255|HAMAP-Rule:MF_00995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O;
CC Xref=Rhea:RHEA:40051, ChEBI:CHEBI:15377, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:76981; EC=4.2.1.151; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00995};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00995, ECO:0000269|PubMed:18801996}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene require menaquinone-4 (MK
CC 4) for their growth. {ECO:0000269|PubMed:18801996}.
CC -!- SIMILARITY: Belongs to the MqnA/MqnD family. MqnA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00995}.
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DR EMBL; AB447888; BAG71674.1; -; Genomic_DNA.
DR EMBL; AL939120; CAB77297.1; -; Genomic_DNA.
DR RefSeq; NP_628670.1; NC_003888.3.
DR RefSeq; WP_003974442.1; NZ_VNID01000017.1.
DR PDB; 2NXO; X-ray; 2.04 A; A/B/C/D=2-282.
DR PDB; 7AHR; X-ray; 2.21 A; A/B=2-282.
DR PDBsum; 2NXO; -.
DR PDBsum; 7AHR; -.
DR AlphaFoldDB; Q9L0T8; -.
DR SMR; Q9L0T8; -.
DR STRING; 100226.SCO4506; -.
DR GeneID; 1099946; -.
DR KEGG; sco:SCO4506; -.
DR PATRIC; fig|100226.15.peg.4579; -.
DR eggNOG; COG1427; Bacteria.
DR HOGENOM; CLU_059898_0_0_11; -.
DR InParanoid; Q9L0T8; -.
DR OMA; WGLARTG; -.
DR PhylomeDB; Q9L0T8; -.
DR BioCyc; MetaCyc:MON-14866; -.
DR BRENDA; 4.2.1.151; 5998.
DR UniPathway; UPA00079; -.
DR EvolutionaryTrace; Q9L0T8; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00995; MqnA; 1.
DR InterPro; IPR003773; Menaquinone_biosynth.
DR InterPro; IPR030868; MqnA.
DR PANTHER; PTHR37690; PTHR37690; 1.
DR Pfam; PF02621; VitK2_biosynth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..282
FT /note="Chorismate dehydratase"
FT /id="PRO_0000425124"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:7AHR"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:7AHR"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:2NXO"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:2NXO"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:2NXO"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:2NXO"
SQ SEQUENCE 282 AA; 31358 MW; 687DB770ABC7BDB6 CRC64;
MDNSRTRPRV GHIQFLNCLP LYWGLARTGT LLDFELTKDT PEKLSEQLVR GDLDIGPVTL
VEFLKNADDL VAFPDIAVGC DGPVMSCVIV SQVPLDRLDG ARVALGSTSR TSVRLAQLLL
SERFGVQPDY YTCPPDLSLM MQEADAAVLI GDAALRANMI DGPRYGLDVH DLGALWKEWT
GLPFVFAVWA ARRDYAEREP VITRKVHEAF LASRNLSLEE VEKVAEQAAR WEAFDEDTLA
KYFTTLDFRF GAPQLEAVTE FARRVGPTTG FPADVKVELL KP
