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Protein

Chorismate dehydratase

Gene

mqnA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).UniRule annotation

Catalytic activityi

Chorismate = 3-((1-carboxyvinyl)oxy)benzoate + H2O.UniRule annotation

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Menaquinone biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14866.
BRENDAi4.2.1.151. 5998.
UniPathwayiUPA00079.

Names & Taxonomyi

Protein namesi
Recommended name:
Chorismate dehydrataseUniRule annotation (EC:4.2.1.151UniRule annotation)
Alternative name(s):
Menaquinone biosynthetic enzyme MqnAUniRule annotation
Gene namesi
Name:mqnAUniRule annotation
Ordered Locus Names:SCO4506
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene require menaquinone-4 (MK 4) for their growth.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004251241 – 282Chorismate dehydrataseAdd BLAST282

Proteomic databases

PRIDEiQ9L0T8.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO4506.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Helixi16 – 18Combined sources3
Helixi19 – 27Combined sources9
Helixi30 – 33Combined sources4
Beta strandi35 – 39Combined sources5
Helixi41 – 49Combined sources9
Beta strandi54 – 59Combined sources6
Helixi60 – 65Combined sources6
Helixi66 – 69Combined sources4
Beta strandi70 – 82Combined sources13
Beta strandi85 – 93Combined sources9
Beta strandi99 – 106Combined sources8
Helixi111 – 122Combined sources12
Beta strandi129 – 133Combined sources5
Beta strandi148 – 150Combined sources3
Helixi151 – 159Combined sources9
Helixi161 – 164Combined sources4
Beta strandi168 – 171Combined sources4
Helixi172 – 180Combined sources9
Beta strandi184 – 192Combined sources9
Helixi193 – 198Combined sources6
Helixi200 – 219Combined sources20
Helixi221 – 229Combined sources9
Beta strandi232 – 234Combined sources3
Helixi236 – 245Combined sources10
Helixi252 – 265Combined sources14
Turni267 – 270Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NXOX-ray2.04A/B/C/D2-282[»]
ProteinModelPortaliQ9L0T8.
SMRiQ9L0T8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9L0T8.

Family & Domainsi

Sequence similaritiesi

Belongs to the MqnA/MqnD family. MqnA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EV6. Bacteria.
COG1427. LUCA.
HOGENOMiHOG000016345.
InParanoidiQ9L0T8.
KOiK11782.
OMAiWGLARTG.
OrthoDBiPOG091H0D1B.
PhylomeDBiQ9L0T8.

Family and domain databases

HAMAPiMF_00995. MqnA. 1 hit.
InterProiIPR003773. Menaquinone_biosynth.
IPR030868. MqnA.
[Graphical view]
PfamiPF02621. VitK2_biosynth. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9L0T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNSRTRPRV GHIQFLNCLP LYWGLARTGT LLDFELTKDT PEKLSEQLVR
60 70 80 90 100
GDLDIGPVTL VEFLKNADDL VAFPDIAVGC DGPVMSCVIV SQVPLDRLDG
110 120 130 140 150
ARVALGSTSR TSVRLAQLLL SERFGVQPDY YTCPPDLSLM MQEADAAVLI
160 170 180 190 200
GDAALRANMI DGPRYGLDVH DLGALWKEWT GLPFVFAVWA ARRDYAEREP
210 220 230 240 250
VITRKVHEAF LASRNLSLEE VEKVAEQAAR WEAFDEDTLA KYFTTLDFRF
260 270 280
GAPQLEAVTE FARRVGPTTG FPADVKVELL KP
Length:282
Mass (Da):31,358
Last modified:October 1, 2000 - v1
Checksum:i687DB770ABC7BDB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB447888 Genomic DNA. Translation: BAG71674.1.
AL939120 Genomic DNA. Translation: CAB77297.1.
RefSeqiNP_628670.1. NC_003888.3.
WP_003974442.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB77297; CAB77297; CAB77297.
GeneIDi1099946.
KEGGisco:SCO4506.
PATRICi23738830. VBIStrCoe124346_4579.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB447888 Genomic DNA. Translation: BAG71674.1.
AL939120 Genomic DNA. Translation: CAB77297.1.
RefSeqiNP_628670.1. NC_003888.3.
WP_003974442.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NXOX-ray2.04A/B/C/D2-282[»]
ProteinModelPortaliQ9L0T8.
SMRiQ9L0T8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO4506.

Proteomic databases

PRIDEiQ9L0T8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB77297; CAB77297; CAB77297.
GeneIDi1099946.
KEGGisco:SCO4506.
PATRICi23738830. VBIStrCoe124346_4579.

Phylogenomic databases

eggNOGiENOG4105EV6. Bacteria.
COG1427. LUCA.
HOGENOMiHOG000016345.
InParanoidiQ9L0T8.
KOiK11782.
OMAiWGLARTG.
OrthoDBiPOG091H0D1B.
PhylomeDBiQ9L0T8.

Enzyme and pathway databases

UniPathwayiUPA00079.
BioCyciMetaCyc:MONOMER-14866.
BRENDAi4.2.1.151. 5998.

Miscellaneous databases

EvolutionaryTraceiQ9L0T8.

Family and domain databases

HAMAPiMF_00995. MqnA. 1 hit.
InterProiIPR003773. Menaquinone_biosynth.
IPR030868. MqnA.
[Graphical view]
PfamiPF02621. VitK2_biosynth. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMQNA_STRCO
AccessioniPrimary (citable) accession number: Q9L0T8
Secondary accession number(s): B5MG03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.