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Protein

4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5

Gene

THI5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.1 Publication

Cofactori

Fe cation1 Publication

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei661 Publication1

GO - Biological processi

  • thiamine biosynthetic process Source: SGD
  • thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Iron, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-3915.
YEAST:MONOMER3O-3915.
UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI51 Publication
Short name:
HMP-P synthase1 Publication
Short name:
Hydroxymethylpyrimidine phosphate synthaseCurated
Alternative name(s):
Thiamine biosynthesis protein 51 Publication
Thiamine pyrimidine synthaseBy similarity
Gene namesi
Name:THI51 Publication
Synonyms:MOL21 Publication
Ordered Locus Names:YFL058WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFL058W.
SGDiS000001836. THI5.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11N → A: Unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi12W → A: Unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi62K → A: Unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi66H → A: Unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi195C → A: Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi196C → A: Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi197C → A: Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. 1 Publication1
Mutagenesisi199C → A: Attenuates the coordination of ion and is unable to sustain growth in thiamine-free medium. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002116181 – 3404-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5Add BLAST340

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei62N6-(pyridoxal phosphate)lysine1 Publication1

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-19221,EBI-16219

Protein-protein interaction databases

BioGridi31089. 3 interactors.
DIPiDIP-3951N.
IntActiP43534. 1 interactor.
MINTiMINT-525063.

Structurei

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Beta strandi11 – 13Combined sources3
Helixi16 – 18Combined sources3
Helixi19 – 26Combined sources8
Helixi29 – 32Combined sources4
Beta strandi37 – 44Combined sources8
Helixi45 – 47Combined sources3
Helixi48 – 54Combined sources7
Beta strandi55 – 57Combined sources3
Beta strandi59 – 63Combined sources5
Helixi64 – 71Combined sources8
Turni72 – 74Combined sources3
Beta strandi77 – 84Combined sources8
Beta strandi89 – 94Combined sources6
Turni95 – 98Combined sources4
Helixi103 – 106Combined sources4
Beta strandi110 – 113Combined sources4
Helixi117 – 127Combined sources11
Turni128 – 130Combined sources3
Beta strandi135 – 140Combined sources6
Helixi142 – 144Combined sources3
Helixi145 – 150Combined sources6
Beta strandi153 – 160Combined sources8
Turni161 – 163Combined sources3
Helixi164 – 174Combined sources11
Helixi179 – 181Combined sources3
Beta strandi182 – 186Combined sources5
Beta strandi192 – 194Combined sources3
Helixi196 – 199Combined sources4
Beta strandi201 – 206Combined sources6
Helixi207 – 212Combined sources6
Helixi214 – 233Combined sources20
Helixi235 – 245Combined sources11
Helixi247 – 249Combined sources3
Helixi252 – 261Combined sources10
Turni262 – 264Combined sources3
Helixi273 – 285Combined sources13
Helixi315 – 330Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4H65X-ray2.60A/B1-340[»]
4H67X-ray2.70A/B/C/D/E/F/G/H1-340[»]
4H6DX-ray2.90A/B/C/D/E/F/G/H1-340[»]
ProteinModelPortaliP43534.
SMRiP43534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 118Pyridoxal phosphate binding1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi195 – 199CCCFC; essential for catalytic activity, may be the site of iron coordination1 Publication5

Sequence similaritiesi

Belongs to the NMT1/THI5 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017029.
HOGENOMiHOG000160891.
InParanoidiP43534.
KOiK18278.
OMAiWFLNADH.
OrthoDBiEOG092C349S.

Family and domain databases

InterProiIPR027939. NMT1/THI5.
IPR015168. SsuA/THI5.
[Graphical view]
PANTHERiPTHR31528. PTHR31528. 1 hit.
PfamiPF09084. NMT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTDKITFLL NWQPTPYHIP IFLAQTKGYF KEQGLDMAIL EPTNPSDVTE
60 70 80 90 100
LIGSGKVDMG LKAMIHTLAA KARGFPVTSV ASLLDEPFTG VLYLKGSGIT
110 120 130 140 150
EDFQSLKGKK IGYVGEFGKI QIDELTKHYG MKPEDYTAVR CGMNVAKYII
160 170 180 190 200
EGKIDAGIGI ECMQQVELEE YLAKQGRPAS DAKMLRIDKL ACLGCCCFCT
210 220 230 240 250
VLYICNDEFL KKNPEKVRKF LKAIKKATDY VLADPVKAWK EYIDFKPQLN
260 270 280 290 300
NDLSYKQYQR CYAYFSSSLY NVHRDWKKVT GYGKRLAILP PDYVSNYTNE
310 320 330 340
YLSWPEPEEV SDPLEAQRLM AIHQEKCRQE GTFKRLALPA
Length:340
Mass (Da):38,592
Last modified:November 1, 1995 - v1
Checksum:iD810C5D5A86FA6C0
GO

Mass spectrometryi

Molecular mass is 38513.4 Da from positions 1 - 340. Determined by ESI. This mass is that of the untagged protein plus the mass of an iron ion.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48220 Genomic DNA. Translation: CAA88253.1.
D50617 Genomic DNA. Translation: BAA09183.1.
BK006940 Genomic DNA. Translation: DAA12382.1.
RefSeqiNP_116597.1. NM_001179909.1.

Genome annotation databases

EnsemblFungiiBAA09183; BAA09183; BAA09183.
YFL058W; YFL058W; YFL058W.
GeneIDi850486.
KEGGisce:YFL058W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48220 Genomic DNA. Translation: CAA88253.1.
D50617 Genomic DNA. Translation: BAA09183.1.
BK006940 Genomic DNA. Translation: DAA12382.1.
RefSeqiNP_116597.1. NM_001179909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4H65X-ray2.60A/B1-340[»]
4H67X-ray2.70A/B/C/D/E/F/G/H1-340[»]
4H6DX-ray2.90A/B/C/D/E/F/G/H1-340[»]
ProteinModelPortaliP43534.
SMRiP43534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31089. 3 interactors.
DIPiDIP-3951N.
IntActiP43534. 1 interactor.
MINTiMINT-525063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09183; BAA09183; BAA09183.
YFL058W; YFL058W; YFL058W.
GeneIDi850486.
KEGGisce:YFL058W.

Organism-specific databases

EuPathDBiFungiDB:YFL058W.
SGDiS000001836. THI5.

Phylogenomic databases

GeneTreeiENSGT00390000017029.
HOGENOMiHOG000160891.
InParanoidiP43534.
KOiK18278.
OMAiWFLNADH.
OrthoDBiEOG092C349S.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciMetaCyc:MONOMER3O-3915.
YEAST:MONOMER3O-3915.

Miscellaneous databases

PROiP43534.

Family and domain databases

InterProiIPR027939. NMT1/THI5.
IPR015168. SsuA/THI5.
[Graphical view]
PANTHERiPTHR31528. PTHR31528. 1 hit.
PfamiPF09084. NMT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHI5_YEAST
AccessioniPrimary (citable) accession number: P43534
Secondary accession number(s): D6VTH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

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.