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P39890

- TCMI_STRGA

UniProt

P39890 - TCMI_STRGA

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Protein

Tetracenomycin F2 cyclase

Gene

tcmI

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

Functioni

Catalyzing the conversion of tetracenomycin F2 to tetracenomycin F1.1 Publication

Catalytic activityi

Tetracenomycin F2 = tetracenomycin F1 + H2O.1 Publication

Kineticsi

  1. KM=121 µM for tetracenomycin F21 Publication

Vmax=704 nmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6-6.5.1 Publication

Pathwayi

GO - Molecular functioni

  1. lyase activity Source: UniProtKB-KW

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
  2. polyketide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18608.
UniPathwayiUPA00174.

Names & Taxonomyi

Protein namesi
Recommended name:
Tetracenomycin F2 cyclase (EC:4.2.1.154)
Alternative name(s):
Tetracenomycin polyketide synthesis protein TcmI
Gene namesi
Name:tcmI
OrganismiStreptomyces glaucescens
Taxonomic identifieri1907 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261H → A: Relative activity reduced to 15% of wild-type. 1 Publication
Mutagenesisi26 – 261H → Q: No effect. 1 Publication
Mutagenesisi27 – 271D → N: Relative activity reduced to 14% of wild-type. 1 Publication
Mutagenesisi40 – 401R → G: Relative activity reduced to 10% of wild-type. 1 Publication
Mutagenesisi40 – 401R → K: Relative activity reduced to 16% of wild-type. 1 Publication
Mutagenesisi51 – 511H → A: Relative activity reduced to 16% of wild-type. 1 Publication
Mutagenesisi51 – 511H → Q: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 109108Tetracenomycin F2 cyclasePRO_0000072454Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi13 – 153Combined sources
Helixi16 – 2611Combined sources
Helixi31 – 355Combined sources
Beta strandi39 – 457Combined sources
Beta strandi48 – 5710Combined sources
Helixi60 – 656Combined sources
Helixi70 – 723Combined sources
Helixi73 – 808Combined sources
Beta strandi83 – 875Combined sources
Helixi93 – 964Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TUWX-ray1.90A1-109[»]
ProteinModelPortaliP39890.
SMRiP39890. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39890.

Family & Domainsi

Family and domain databases

Gene3Di3.30.70.1090. 1 hit.
InterProiIPR011008. Dimeric_a/b-barrel.
IPR006765. Polyketide_synth_cyclase.
[Graphical view]
PfamiPF04673. Cyclase_polyket. 1 hit.
[Graphical view]
ProDomiPD012644. Polyketide_synth_cyclase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54909. SSF54909. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39890-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAYRALMVLR MDPADAEHVA AAFAEHDTTE LPLEIGVRRR VLFRFHDLYM
60 70 80 90 100
HLIEADDDIM ERLYQARSHP LFQEVNERVG QYLTPYAQDW EELKDSKAEV

FYSWTAPDS
Length:109
Mass (Da):12,861
Last modified:February 1, 1995 - v1
Checksum:i1F9E3EC9E1B90593
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80674 Genomic DNA. Translation: AAA67513.1.
PIRiB53291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80674 Genomic DNA. Translation: AAA67513.1 .
PIRi B53291.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TUW X-ray 1.90 A 1-109 [» ]
ProteinModelPortali P39890.
SMRi P39890. Positions 2-107.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00174 .
BioCyci MetaCyc:MONOMER-18608.

Miscellaneous databases

EvolutionaryTracei P39890.

Family and domain databases

Gene3Di 3.30.70.1090. 1 hit.
InterProi IPR011008. Dimeric_a/b-barrel.
IPR006765. Polyketide_synth_cyclase.
[Graphical view ]
Pfami PF04673. Cyclase_polyket. 1 hit.
[Graphical view ]
ProDomi PD012644. Polyketide_synth_cyclase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF54909. SSF54909. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Sequence and transcriptional analysis of the Streptomyces glaucescens tcmAR tetracenomycin C resistance and repressor gene loci."
    Guilfoile P.G., Hutchinson C.R.
    J. Bacteriol. 174:3651-3658(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 40716 / ETH 22794 / GLA.0.
  2. "Tetracenomycin F2 cyclase: intramolecular aldol condensation in the biosynthesis of tetracenomycin C in Streptomyces glaucescens."
    Shen B., Hutchinson C.R.
    Biochemistry 32:11149-11154(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: WMH1068.
  3. "Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase."
    Thompson T.B., Katayama K., Watanabe K., Hutchinson C.R., Rayment I.
    J. Biol. Chem. 279:37956-37963(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, MUTAGENESIS OF HIS-26; ASP-27; ARG-40 AND HIS-51.

Entry informationi

Entry nameiTCMI_STRGA
AccessioniPrimary (citable) accession number: P39890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 58 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, Direct protein sequencing

Documents

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

External Data

Dasty 3