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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)DescriptionActionsGraphical viewLength
Active sitei63Proton donor/acceptor1 Publication1
Binding sitei93Substrate1 Publication1
Binding sitei205Substrate1 Publication1
Binding sitei311Substrate1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi63Y → F: Complete loss of activity. It does not affect the over-all structure of the enzyme. 1 Publication1
Mutagenesisi71E → A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine. 1 Publication1
Mutagenesisi93H → F: Complete loss of activity. 1 Publication1
Mutagenesisi303Y → A: Despite a decrease in activity, it shows lyase activity over time and still produced some amount of beta-tyrosine. 1 Publication1
Mutagenesisi415Y → V: Complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004241971 – 539MIO-dependent tyrosine 2,3-aminomutaseAdd BLAST539

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki152 ↔ 1545-imidazolinone (Ala-Gly)Curated
Modified residuei1532,3-didehydroalanine (Ser)Curated1

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

1539
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Helixi22 – 30Combined sources9
Helixi39 – 56Combined sources18
Turni57 – 59Combined sources3
Turni63 – 65Combined sources3
Helixi70 – 74Combined sources5
Beta strandi75 – 77Combined sources3
Helixi79 – 81Combined sources3
Helixi82 – 92Combined sources11
Beta strandi97 – 100Combined sources4
Helixi103 – 117Combined sources15
Helixi126 – 137Combined sources12
Beta strandi145 – 147Combined sources3
Beta strandi151 – 154Combined sources4
Helixi156 – 166Combined sources11
Beta strandi170 – 174Combined sources5
Beta strandi177 – 180Combined sources4
Helixi181 – 186Combined sources6
Turni187 – 189Combined sources3
Helixi199 – 204Combined sources6
Beta strandi205 – 207Combined sources3
Helixi208 – 238Combined sources31
Helixi244 – 246Combined sources3
Helixi248 – 250Combined sources3
Turni251 – 254Combined sources4
Helixi258 – 271Combined sources14
Beta strandi275 – 278Combined sources4
Helixi280 – 290Combined sources11
Beta strandi296 – 298Combined sources3
Helixi308 – 310Combined sources3
Helixi313 – 335Combined sources23
Beta strandi341 – 343Combined sources3
Helixi359 – 387Combined sources29
Turni389 – 391Combined sources3
Beta strandi392 – 394Combined sources3
Helixi397 – 399Combined sources3
Helixi411 – 424Combined sources14
Turni438 – 441Combined sources4
Helixi448 – 480Combined sources33
Helixi483 – 485Combined sources3
Helixi488 – 500Combined sources13
Helixi511 – 522Combined sources12
Helixi525 – 533Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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: November 2, 2016
This is version 81 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.