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Protein

Mycinamicin VI 2''-O-methyltransferase

Gene

mycE

Organism
Micromonospora griseorubida
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

O-methyltransferase that catalyzes the conversion of mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + mycinamicin VI = S-adenosyl-L-homocysteine + mycinamicin III.2 Publications

Cofactori

Mg2+2 Publications

Pathwayi: mycinamicin biosynthesis

This protein is involved in the pathway mycinamicin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway mycinamicin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731S-adenosyl-L-methionine1 Publication
Binding sitei217 – 2171S-adenosyl-L-methionine1 Publication
Binding sitei234 – 2341S-adenosyl-L-methionine1 Publication
Metal bindingi275 – 2751Magnesium1 Publication
Binding sitei275 – 2751S-adenosyl-L-methionine1 Publication
Active sitei278 – 2781Proton acceptor1 Publication
Metal bindingi303 – 3031Magnesium1 Publication
Metal bindingi304 – 3041Magnesium1 Publication

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB
  • mycinamicin VI 2''-O-methyltransferase activity Source: UniProtKB-EC
  • O-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • antibiotic biosynthetic process Source: UniProtKB
  • methylation Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18367.
BRENDAi2.1.1.238. 7845.
UniPathwayiUPA01019.

Names & Taxonomyi

Protein namesi
Recommended name:
Mycinamicin VI 2''-O-methyltransferaseCurated (EC:2.1.1.2382 Publications)
Alternative name(s):
Mycinamicin biosynthesis protein E
Gene namesi
Name:mycE
OrganismiMicromonospora griseorubida
Taxonomic identifieri28040 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeMicromonospora

Pathology & Biotechi

Disruption phenotypei

No production of mycinamicin II and accumulation of mycinamicin VI.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081Y → F: Decreased catalytic activity. 1 Publication
Mutagenesisi278 – 2781H → A, K or Q: Abolishes catalytic activity. 1 Publication
Mutagenesisi279 – 2791I → V: Slightly increased catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Mycinamicin VI 2''-O-methyltransferasePRO_0000418457Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi23 – 3210Combined sources
Helixi35 – 4915Combined sources
Beta strandi59 – 679Combined sources
Beta strandi70 – 789Combined sources
Beta strandi85 – 873Combined sources
Beta strandi94 – 1018Combined sources
Helixi102 – 1109Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi122 – 1265Combined sources
Helixi135 – 15521Combined sources
Helixi164 – 1707Combined sources
Beta strandi176 – 1794Combined sources
Helixi183 – 1908Combined sources
Helixi191 – 1933Combined sources
Beta strandi199 – 2035Combined sources
Helixi216 – 2249Combined sources
Beta strandi229 – 2368Combined sources
Helixi239 – 2413Combined sources
Beta strandi246 – 2505Combined sources
Helixi256 – 26611Combined sources
Beta strandi269 – 2746Combined sources
Helixi280 – 29011Combined sources
Helixi291 – 2933Combined sources
Beta strandi294 – 30310Combined sources
Helixi305 – 3095Combined sources
Helixi326 – 33712Combined sources
Helixi339 – 3413Combined sources
Helixi352 – 3565Combined sources
Beta strandi357 – 3637Combined sources
Beta strandi366 – 3727Combined sources
Helixi387 – 3948Combined sources
Turni395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SSMX-ray2.25A/B/C/D1-399[»]
3SSNX-ray2.39A/B/C/D1-399[»]
3SSOX-ray1.90A/B/C/D/E/F1-399[»]
ProteinModelPortaliQ83WF2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni202 – 2087S-adenosyl-L-methionine binding1 Publication
Regioni252 – 2532S-adenosyl-L-methionine binding1 Publication

Sequence similaritiesi

Belongs to the methyltransferase OleY/MycE family.Curated

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q83WF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAQTEFDEA TVQDVVRLAG GHDSELRELT QKYDPAMISR LLVAEILSRC
60 70 80 90 100
PPPSNDTPVL VELAIVHGSE RFRHFLRVVR DSPIRPVGAD EGFVGMLVEY
110 120 130 140 150
ELTELLRELF GVTHERPAGV RGTKLFPYLT DDEEAVEQIG TYLLAAQQGT
160 170 180 190 200
EAVLAGCGSR KPDLSELSSR YFTPKFGFLH WFTPHYDRHF RDYRNQQVRV
210 220 230 240 250
LEIGVGGYKH PEWGGGSLRM WKSFFPRGQI YGLDIMDKSH VDELRIRTIQ
260 270 280 290 300
GDQNDAEFLD RIARRYGPFD IVIDDGSHIN AHVRTSFAAL FPHVRPGGLY
310 320 330 340 350
VIEDMWTAYW PGFGGQADPQ ECSGTSLGLL KSLIDAIQHQ ELPSDPNRSP
360 370 380 390
GYVDRNIVGL HVYHNVAFVE KGRNDEGGIP TWIPRDFESL VQASSGGAT
Length:399
Mass (Da):44,809
Last modified:June 1, 2003 - v1
Checksum:iD608846BD0F5A012
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089954 Genomic DNA. Translation: BAC57026.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089954 Genomic DNA. Translation: BAC57026.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SSMX-ray2.25A/B/C/D1-399[»]
3SSNX-ray2.39A/B/C/D1-399[»]
3SSOX-ray1.90A/B/C/D/E/F1-399[»]
ProteinModelPortaliQ83WF2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA01019.
BioCyciMetaCyc:MONOMER-18367.
BRENDAi2.1.1.238. 7845.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMYCE_MICGR
AccessioniPrimary (citable) accession number: Q83WF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: June 1, 2003
Last modified: September 7, 2016
This is version 37 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

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.