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Protein

Uric acid degradation bifunctional protein TTL

Gene

TTL

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the last two steps of the degradation of uric acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its stereoselective decarboxylation to (S)-allantoin. Might function as a negative regulator to modulate brassinosteroid-mediated plant growth.

Catalytic activityi

5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate.
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2.

Pathwayi: urate degradation

This protein is involved in step 2 and 3 of the subpathway that synthesizes (S)-allantoin from urate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Uricase (At2g26230)
  2. Uric acid degradation bifunctional protein TTL (TTL)
  3. Uric acid degradation bifunctional protein TTL (TTL)
This subpathway is part of the pathway urate degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Proton donor; for OHCU decarboxylase activity
Binding sitei80 – 801Substrate

GO - Molecular functioni

  • 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity Source: TAIR
  • hydroxyisourate hydrolase activity Source: TAIR

GO - Biological processi

  • allantoin biosynthetic process Source: TAIR
  • brassinosteroid mediated signaling pathway Source: TAIR
  • protein homotetramerization Source: TAIR
  • purine nucleobase metabolic process Source: UniProtKB-KW
  • regulation of cell growth by extracellular stimulus Source: TAIR
  • urate catabolic process Source: UniProtKB-UniPathway

Keywords - Molecular functioni

Decarboxylase, Hydrolase, Lyase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BioCyciARA:AT5G58220-MONOMER.
ARA:GQT-2131-MONOMER.
ARA:GQT-2730-MONOMER.
MetaCyc:AT5G58220-MONOMER.
BRENDAi4.1.1.97. 399.
UniPathwayiUPA00394; UER00651.
UPA00394; UER00652.

Protein family/group databases

TCDBi9.B.35.1.3. the putative thyronine-transporting transthyretin (transthyretin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Uric acid degradation bifunctional protein TTL
Alternative name(s):
Transthyretin-like protein
Including the following 2 domains:
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (EC:4.1.1.97)
Short name:
OHCU decarboxylase
5-hydroxyisourate hydrolase (EC:3.5.2.17)
Short name:
HIU hydrolase
Short name:
HIUHase
Gene namesi
Name:TTL
Ordered Locus Names:At5g58220
ORF Names:MCK7.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G58220.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • extrinsic component of cytoplasmic side of plasma membrane Source: TAIR
  • peroxisome Source: TAIR

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 324323Uric acid degradation bifunctional protein TTLPRO_0000050606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Post-translational modificationi

Phosphorylated by BRI1 in vitro.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9LVM5.
PRIDEiQ9LVM5.

PTM databases

iPTMnetiQ9LVM5.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Inductioni

Not regulated by plant steroids.

Gene expression databases

ExpressionAtlasiQ9LVM5. baseline and differential.
GenevisibleiQ9LVM5. AT.

Interactioni

Subunit structurei

Interacts with BRI1. Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRI1O224763EBI-1803584,EBI-1797828

Protein-protein interaction databases

BioGridi21178. 4 interactions.
IntActiQ9LVM5. 1 interaction.
STRINGi3702.AT5G58220.1.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi13 – 153Combined sources
Helixi17 – 248Combined sources
Helixi31 – 4414Combined sources
Helixi48 – 569Combined sources
Helixi82 – 854Combined sources
Helixi90 – 10718Combined sources
Helixi120 – 13011Combined sources
Helixi135 – 15824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q37X-ray2.50A1-161[»]
ProteinModelPortaliQ9LVM5.
SMRiQ9LVM5. Positions 6-160, 205-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LVM5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 161160OHCU decarboxylaseAdd
BLAST
Regioni58 – 592Substrate binding
Regioni111 – 1155Substrate binding
Regioni178 – 324147HIU hydrolaseAdd
BLAST

Domaini

The N-terminal 29 amino acids are essential, but not sufficient, for the interaction with BRI1.

Sequence similaritiesi

In the N-terminal section; belongs to the OHCU decarboxylase family.Curated
In the C-terminal section; belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.Curated

Phylogenomic databases

eggNOGiKOG3006. Eukaryota.
COG2351. LUCA.
HOGENOMiHOG000012804.
InParanoidiQ9LVM5.
KOiK13484.
OMAiLACCGST.
PhylomeDBiQ9LVM5.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
2.60.40.180. 1 hit.
InterProiIPR017129. HIU_hydrol/OHCU_decarb.
IPR014306. Hydroxyisourate_hydrolase.
IPR018020. OHCU_decarboxylase.
IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
PF00576. Transthyretin. 1 hit.
[Graphical view]
PIRSFiPIRSF037178. UCP037178_transthyretin. 1 hit.
PRINTSiPR00189. TRNSTHYRETIN.
SUPFAMiSSF49472. SSF49472. 1 hit.
TIGRFAMsiTIGR02962. hdxy_isourate. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9LVM5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAMEIGEDEW KVCCGSSEFA KQMSTSGPLT SQEAIYTARD IWFNQVNVTD
60 70 80 90 100
WLEAFSAHPQ IGNTPSPSIN SDFARRSVSE QSTAFATTSA SALQELAEWN
110 120 130 140 150
VLYKKKFGFI FIICASGRTH AEMLHALKER YENRPIVELE IAAMEQMKIT
160 170 180 190 200
ELRMAKLFSD KAKVISETDS SSSPVSTKPQ DRLRIIGGHL NVAAEAKAPK
210 220 230 240 250
RSRPPITTHV LDVSRGAPAA GVEVHLEVWS GTTGPSFVHG GGGVWSSVGT
260 270 280 290 300
SATDRDGRSG PLMDLVDALN PGTYRISFDT AKYSPGCFFP YVSIVFQVTE
310 320
SQKWEHFHVP LLLAPFSFST YRGS
Length:324
Mass (Da):35,564
Last modified:October 1, 2000 - v1
Checksum:i99191F450BDE262F
GO
Isoform 2 (identifier: Q9LVM5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-193: Missing.

Show »
Length:311
Mass (Da):34,149
Checksum:i00ED64B2F3754488
GO
Isoform 3 (identifier: Q9LVM5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-218: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:286
Mass (Da):31,511
Checksum:iC1B44222CCEF63D2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei181 – 21838Missing in isoform 3. CuratedVSP_030135Add
BLAST
Alternative sequencei181 – 19313Missing in isoform 2. 1 PublicationVSP_030136Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019228 Genomic DNA. Translation: BAA96913.1.
CP002688 Genomic DNA. Translation: AED97018.1.
CP002688 Genomic DNA. Translation: AED97019.1.
CP002688 Genomic DNA. Translation: AED97020.1.
AY062771 mRNA. Translation: AAL32849.1.
AY081647 mRNA. Translation: AAM10209.1.
AK226943 mRNA. Translation: BAE99013.1.
RefSeqiNP_001032093.1. NM_001037016.2. [Q9LVM5-3]
NP_001032094.1. NM_001037017.2. [Q9LVM5-2]
NP_200630.1. NM_125207.4. [Q9LVM5-1]
UniGeneiAt.27237.

Genome annotation databases

EnsemblPlantsiAT5G58220.1; AT5G58220.1; AT5G58220. [Q9LVM5-1]
GeneIDi835934.
KEGGiath:AT5G58220.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019228 Genomic DNA. Translation: BAA96913.1.
CP002688 Genomic DNA. Translation: AED97018.1.
CP002688 Genomic DNA. Translation: AED97019.1.
CP002688 Genomic DNA. Translation: AED97020.1.
AY062771 mRNA. Translation: AAL32849.1.
AY081647 mRNA. Translation: AAM10209.1.
AK226943 mRNA. Translation: BAE99013.1.
RefSeqiNP_001032093.1. NM_001037016.2. [Q9LVM5-3]
NP_001032094.1. NM_001037017.2. [Q9LVM5-2]
NP_200630.1. NM_125207.4. [Q9LVM5-1]
UniGeneiAt.27237.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q37X-ray2.50A1-161[»]
ProteinModelPortaliQ9LVM5.
SMRiQ9LVM5. Positions 6-160, 205-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21178. 4 interactions.
IntActiQ9LVM5. 1 interaction.
STRINGi3702.AT5G58220.1.

Protein family/group databases

TCDBi9.B.35.1.3. the putative thyronine-transporting transthyretin (transthyretin) family.

PTM databases

iPTMnetiQ9LVM5.

Proteomic databases

PaxDbiQ9LVM5.
PRIDEiQ9LVM5.

Protocols and materials databases

DNASUi835934.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G58220.1; AT5G58220.1; AT5G58220. [Q9LVM5-1]
GeneIDi835934.
KEGGiath:AT5G58220.

Organism-specific databases

TAIRiAT5G58220.

Phylogenomic databases

eggNOGiKOG3006. Eukaryota.
COG2351. LUCA.
HOGENOMiHOG000012804.
InParanoidiQ9LVM5.
KOiK13484.
OMAiLACCGST.
PhylomeDBiQ9LVM5.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00651.
UPA00394; UER00652.
BioCyciARA:AT5G58220-MONOMER.
ARA:GQT-2131-MONOMER.
ARA:GQT-2730-MONOMER.
MetaCyc:AT5G58220-MONOMER.
BRENDAi4.1.1.97. 399.

Miscellaneous databases

EvolutionaryTraceiQ9LVM5.
PROiQ9LVM5.

Gene expression databases

ExpressionAtlasiQ9LVM5. baseline and differential.
GenevisibleiQ9LVM5. AT.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
2.60.40.180. 1 hit.
InterProiIPR017129. HIU_hydrol/OHCU_decarb.
IPR014306. Hydroxyisourate_hydrolase.
IPR018020. OHCU_decarboxylase.
IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
PF00576. Transthyretin. 1 hit.
[Graphical view]
PIRSFiPIRSF037178. UCP037178_transthyretin. 1 hit.
PRINTSiPR00189. TRNSTHYRETIN.
SUPFAMiSSF49472. SSF49472. 1 hit.
TIGRFAMsiTIGR02962. hdxy_isourate. 1 hit.
PROSITEiPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Arabidopsis transthyretin-like protein is a potential substrate of BRASSINOSTEROID-INSENSITIVE 1."
    Nam K.H., Li J.
    Plant Cell 16:2406-2417(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BRI1.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  6. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structural and functional basis for (S)-allantoin formation in the ureide pathway."
    Kim K., Park J., Rhee S.
    J. Biol. Chem. 282:23457-23464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-161 IN COMPLEX WITH (S)-ALLANTOIN, SUBUNIT, REACTION MECHANISM.

Entry informationi

Entry nameiTTHL_ARATH
AccessioniPrimary (citable) accession number: Q9LVM5
Secondary accession number(s): Q2V2X6, Q2V2X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.