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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)DescriptionActionsGraphical viewLength
Binding sitei173S-adenosyl-L-methionine1 Publication1
Binding sitei217S-adenosyl-L-methionine1 Publication1
Binding sitei234S-adenosyl-L-methionine1 Publication1
Metal bindingi275Magnesium1 Publication1
Binding sitei275S-adenosyl-L-methionine1 Publication1
Active sitei278Proton acceptor1 Publication1
Metal bindingi303Magnesium1 Publication1
Metal bindingi304Magnesium1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi208Y → F: Decreased catalytic activity. 1 Publication1
Mutagenesisi278H → A, K or Q: Abolishes catalytic activity. 1 Publication1
Mutagenesisi279I → V: Slightly increased catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004184571 – 399Mycinamicin VI 2''-O-methyltransferaseAdd BLAST399

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 19Combined sources11
Helixi23 – 32Combined sources10
Helixi35 – 49Combined sources15
Beta strandi59 – 67Combined sources9
Beta strandi70 – 78Combined sources9
Beta strandi85 – 87Combined sources3
Beta strandi94 – 101Combined sources8
Helixi102 – 110Combined sources9
Beta strandi117 – 120Combined sources4
Beta strandi122 – 126Combined sources5
Helixi135 – 155Combined sources21
Helixi164 – 170Combined sources7
Beta strandi176 – 179Combined sources4
Helixi183 – 190Combined sources8
Helixi191 – 193Combined sources3
Beta strandi199 – 203Combined sources5
Helixi216 – 224Combined sources9
Beta strandi229 – 236Combined sources8
Helixi239 – 241Combined sources3
Beta strandi246 – 250Combined sources5
Helixi256 – 266Combined sources11
Beta strandi269 – 274Combined sources6
Helixi280 – 290Combined sources11
Helixi291 – 293Combined sources3
Beta strandi294 – 303Combined sources10
Helixi305 – 309Combined sources5
Helixi326 – 337Combined sources12
Helixi339 – 341Combined sources3
Helixi352 – 356Combined sources5
Beta strandi357 – 363Combined sources7
Beta strandi366 – 372Combined sources7
Helixi387 – 394Combined sources8
Turni395 – 397Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiQ83WF2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni202 – 208S-adenosyl-L-methionine binding1 Publication7
Regioni252 – 253S-adenosyl-L-methionine binding1 Publication2

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
PDB 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.
SMRiQ83WF2.
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: November 2, 2016
This is version 38 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.