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Protein

MIO-dependent tyrosine 2,3-aminomutase

Gene
N/A
Organism
Streptomyces globisporus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the enediyne antitumor antibiotic C-1027. Catalyzes the MIO-dependent deamination of L-tyrosine generating the corresponding alpha,beta-unsaturated acid, (S)-beta-tyrosine.3 Publications

Catalytic activityi

L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate.1 Publication
L-tyrosine = trans-p-hydroxycinnamate + ammonia.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Proton donor/acceptor1 Publication
Binding sitei93 – 931Substrate1 Publication
Binding sitei205 – 2051Substrate1 Publication
Binding sitei311 – 3111Substrate1 Publication

GO - Molecular functioni

  • tyrosine 2,3-aminomutase activity Source: UniProtKB
  • tyrosine ammonia-lyase activity Source: UniProtKB

GO - Biological processi

  • antibiotic biosynthetic process Source: UniProtKB-KW
  • toxin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Antibiotic biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
MIO-dependent tyrosine 2,3-aminomutase (EC:5.4.3.6)
Alternative name(s):
Tyrosine ammonia-lyase (EC:4.3.1.23)
OrganismiStreptomyces globisporus
Taxonomic identifieri1908 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631Y → F: Complete loss of activity. It does not affect the over-all structure of the enzyme. 1 Publication
Mutagenesisi71 – 711E → A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine. 1 Publication
Mutagenesisi93 – 931H → F: Complete loss of activity. 1 Publication
Mutagenesisi303 – 3031Y → A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine. 1 Publication
Mutagenesisi415 – 4151Y → V: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539MIO-dependent tyrosine 2,3-aminomutasePRO_0000424197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki152 ↔ 1545-imidazolinone (Ala-Gly)Curated
Modified residuei153 – 15312,3-didehydroalanine (Ser)Curated

Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.Curated1 Publication

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.3 Publications

Structurei

Secondary structure

1
539
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Helixi22 – 309Combined sources
Helixi39 – 5618Combined sources
Turni57 – 593Combined sources
Turni63 – 653Combined sources
Helixi70 – 745Combined sources
Beta strandi75 – 773Combined sources
Helixi79 – 813Combined sources
Helixi82 – 9211Combined sources
Beta strandi97 – 1004Combined sources
Helixi103 – 11715Combined sources
Helixi126 – 13712Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi151 – 1544Combined sources
Helixi156 – 16611Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi177 – 1804Combined sources
Helixi181 – 1866Combined sources
Turni187 – 1893Combined sources
Helixi199 – 2046Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 23831Combined sources
Helixi244 – 2463Combined sources
Helixi248 – 2503Combined sources
Turni251 – 2544Combined sources
Helixi258 – 27114Combined sources
Beta strandi275 – 2784Combined sources
Helixi280 – 29011Combined sources
Beta strandi296 – 2983Combined sources
Helixi308 – 3103Combined sources
Helixi313 – 33523Combined sources
Beta strandi341 – 3433Combined sources
Helixi359 – 38729Combined sources
Turni389 – 3913Combined sources
Beta strandi392 – 3943Combined sources
Helixi397 – 3993Combined sources
Helixi411 – 42414Combined sources
Turni438 – 4414Combined sources
Helixi448 – 48033Combined sources
Helixi483 – 4853Combined sources
Helixi488 – 50013Combined sources
Helixi511 – 52212Combined sources
Helixi525 – 5339Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OHYX-ray2.50A/B1-539[»]
2QVEX-ray2.00A/B12-539[»]
2RJRX-ray2.10A/B1-539[»]
2RJSX-ray2.40A/B1-539[»]
3KDYX-ray2.20A/B1-539[»]
3KDZX-ray2.20A/B1-539[»]
ProteinModelPortaliQ8GMG0.
SMRiQ8GMG0. Positions 11-539.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GMG0.

Family & Domainsi

Sequence similaritiesi

Belongs to the TAL/TAM family.Curated

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
Gene3Di1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR022314. Tyr_aminomutase.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR03832. Tyr_2_3_mutase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8GMG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTQVETEI VPVSVDGETL TVEAVRRVAE ERATVDVPAE SIAKAQKSRE
60 70 80 90 100
IFEGIAEQNI PIYGVTTGYG EMIYMQVDKS KEVELQTNLV RSHSAGVGPL
110 120 130 140 150
FAEDEARAIV AARLNTLAKG HSAVRPIILE RLAQYLNEGI TPAIPEIGSL
160 170 180 190 200
GASGDLAPLS HVASTLIGEG YVLRDGRPVE TAQVLAERGI EPLELRFKEG
210 220 230 240 250
LALINGTSGM TGLGSLVVGR ALEQAQQAEI VTALLIEAVR GSTSPFLAEG
260 270 280 290 300
HDIARPHEGQ IDTAANMRAL MRGSGLTVEH ADLRRELQKD KEAGKDVQRS
310 320 330 340 350
EIYLQKAYSL RAIPQVVGAV RDTLYHARHK LRIELNSAND NPLFFEGKEI
360 370 380 390 400
FHGANFHGQP IAFAMDFVTI ALTQLGVLAE RQINRVLNRH LSYGLPEFLV
410 420 430 440 450
SGDPGLHSGF AGAQYPATAL VAENRTIGPA STQSVPSNGD NQDVVSMGLI
460 470 480 490 500
SARNARRVLS NNNKILAVEY LAAAQAVDIS GRFDGLSPAA KATYEAVRRL
510 520 530
VPTLGVDRYM ADDIELVADA LSRGEFLRAI ARETDIQLR
Length:539
Mass (Da):58,139
Last modified:March 1, 2003 - v1
Checksum:iE0CE3B75B579B1D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048670 Genomic DNA. Translation: AAL06680.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048670 Genomic DNA. Translation: AAL06680.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OHYX-ray2.50A/B1-539[»]
2QVEX-ray2.00A/B12-539[»]
2RJRX-ray2.10A/B1-539[»]
2RJSX-ray2.40A/B1-539[»]
3KDYX-ray2.20A/B1-539[»]
3KDZX-ray2.20A/B1-539[»]
ProteinModelPortaliQ8GMG0.
SMRiQ8GMG0. Positions 11-539.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GMG0.

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
Gene3Di1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR022314. Tyr_aminomutase.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR03832. Tyr_2_3_mutase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTAM_STRGL
AccessioniPrimary (citable) accession number: Q8GMG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 79 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.