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Protein

Multifunctional cyclase-dehydratase-3-O-methyl transferase TcmN

Gene

tcmN

Organism
Streptomyces glaucescens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The N-terminal domain enhances the formation of an early, partially cyclized intermediate, while the C-terminal domain catalyzes the 3-O-methylation of one or more later intermediates in the biosynthetic pathway. Catalyzes the methylation of tetracenomycin D3 (Tcm D3) to yield Tcm B3. Catalyzes as well the following side reactions: methylation of 8-O-methyl-Tcm D3 to yield Tcm E; and of 9-carboxymethyl-Tcm B3 to yield Tcm A2.

Pathwayi: tetracenomycin C biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei358 – 3581S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei405 – 4051Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18604.
UniPathwayiUPA00174.

Names & Taxonomyi

Protein namesi
Recommended name:
Multifunctional cyclase-dehydratase-3-O-methyl transferase TcmN (EC:2.1.1.-)
Gene namesi
Name:tcmN
OrganismiStreptomyces glaucescens
Taxonomic identifieri1907 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Multifunctional cyclase-dehydratase-3-O-methyl transferase TcmNPRO_0000072456Add
BLAST

Structurei

Secondary structure

1
494
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Helixi15 – 228Combined sources
Helixi25 – 273Combined sources
Helixi28 – 314Combined sources
Beta strandi35 – 4410Combined sources
Beta strandi47 – 548Combined sources
Beta strandi64 – 729Combined sources
Helixi73 – 753Combined sources
Beta strandi77 – 848Combined sources
Beta strandi88 – 10013Combined sources
Beta strandi103 – 11412Combined sources
Helixi122 – 15130Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RERX-ray1.90A1-170[»]
2RESX-ray2.20A1-170[»]
2REZX-ray1.95A1-154[»]
3TVQX-ray1.67A1-169[»]
ProteinModelPortaliP16559.
SMRiP16559. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16559.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni384 – 3863S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Domaini

This multifunction enzyme is comprised of two structurally and functionally independent domains.

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.530.20. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR005031. COQ10_START.
IPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR023393. START-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
PF03364. Polyketide_cyc. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16559-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARTDNSIV VNAPFELVWD VTNDIEAWPE LFSEYAEAEI LRQDGDGFDF
60 70 80 90 100
RLKTRPDANG RVWEWVSHRV PDKGSRTVRA HRVETGPFAY MNLHWTYRAV
110 120 130 140 150
AGGTEMRWVQ EFDMKPGAPF DNAHMTAHLN TTTRANMERI KKIIEDRHRE
160 170 180 190 200
GQRTPASVLP TELHAQQLLL LAASGRLARI VHVLTELRIA DLLADGPRHV
210 220 230 240 250
AELAKETDTH ELSLYRVLRS AASVGVFAEG PVRTFSATPL SDGLRTGNPD
260 270 280 290 300
GVLPLVKYNN MELTRRPYDE IMHSVRTGEP AFRRVFGSSF FEHLEANPEA
310 320 330 340 350
GEFFERFMAH WSRRLVLDGL ADQGMERFSR IADLGGGDGW FLAQILRRHP
360 370 380 390 400
HATGLLMDLP RVAASAGPVL EEAKVADRVT VLPGDFFTDP VPTGYDAYLF
410 420 430 440 450
KGVLHNWSDE RAVTVLRRVR EAIGDDDARL LIFDQVMAPE NEWDHAKLLD
460 470 480 490
IDMLVLFGGR ERVLAEWRQL LLEADFDIVN TPSHTWTTLE CRPV
Length:494
Mass (Da):55,930
Last modified:February 1, 1995 - v2
Checksum:i6E153D32782F66B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80674 Genomic DNA. Translation: AAA67518.1.
X15312 Genomic DNA. Translation: CAB38457.1.
PIRiB42276. S27696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80674 Genomic DNA. Translation: AAA67518.1.
X15312 Genomic DNA. Translation: CAB38457.1.
PIRiB42276. S27696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RERX-ray1.90A1-170[»]
2RESX-ray2.20A1-170[»]
2REZX-ray1.95A1-154[»]
3TVQX-ray1.67A1-169[»]
ProteinModelPortaliP16559.
SMRiP16559. Positions 1-155.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00174.
BioCyciMetaCyc:MONOMER-18604.

Miscellaneous databases

EvolutionaryTraceiP16559.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.530.20. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR005031. COQ10_START.
IPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR023393. START-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
PF03364. Polyketide_cyc. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCMN_STRGA
AccessioniPrimary (citable) accession number: P16559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: December 9, 2015
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

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.