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Protein

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20

Gene

THI20

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

Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.1 Publication

Catalytic activityi

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine = ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.
ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine.

Pathway:ithiamine diphosphate biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21 (THI21), Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20 (THI20)
  3. Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21 (THI21), Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20 (THI20)
This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641SubstrateBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • hydroxymethylpyrimidine kinase activity Source: SGD
  • phosphomethylpyrimidine kinase activity Source: SGD
  • thiaminase activity Source: SGD

GO - Biological processi

  • thiamine biosynthetic process Source: SGD
  • thiamine catabolic process Source: SGD
  • thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-77.
YEAST:MONOMER3O-77.
BRENDAi2.7.1.49. 984.
2.7.4.7. 984.
3.5.99.2. 984.
UniPathwayiUPA00060; UER00137.
UPA00060; UER00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20 (EC:2.7.1.49, EC:2.7.4.7)
Alternative name(s):
Hydroxymethylpyrimidine kinase
Short name:
HMP kinase
Hydroxymethylpyrimidine phosphate kinase
Short name:
HMP-P kinase
Short name:
HMP-phosphate kinase
Short name:
HMPP kinase
Gene namesi
Name:THI20
Ordered Locus Names:YOL055C
ORF Names:O1239
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL055c.
EuPathDBiFungiDB:YOL055C.
SGDiS000005416. THI20.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20PRO_0000192041Add
BLAST

Proteomic databases

MaxQBiQ08224.
PaxDbiQ08224.
PeptideAtlasiQ08224.

Expressioni

Inductioni

By absence of thiamine.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi34346. 17 interactions.
DIPiDIP-8852N.
IntActiQ08224. 1 interaction.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi15 – 184Combined sources
Beta strandi25 – 317Combined sources
Beta strandi36 – 383Combined sources
Helixi39 – 4911Combined sources
Beta strandi53 – 6412Combined sources
Beta strandi69 – 746Combined sources
Helixi77 – 9014Combined sources
Beta strandi94 – 985Combined sources
Helixi103 – 11614Combined sources
Helixi117 – 1193Combined sources
Beta strandi122 – 1254Combined sources
Helixi142 – 1498Combined sources
Helixi151 – 1533Combined sources
Beta strandi155 – 1573Combined sources
Helixi161 – 1688Combined sources
Helixi178 – 19114Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi212 – 2198Combined sources
Turni220 – 2234Combined sources
Beta strandi224 – 2318Combined sources
Helixi241 – 25414Combined sources
Helixi259 – 27618Combined sources
Turni293 – 2964Combined sources
Helixi300 – 3056Combined sources
Helixi333 – 3397Combined sources
Turni341 – 3433Combined sources
Helixi344 – 3518Combined sources
Helixi354 – 3607Combined sources
Helixi366 – 39328Combined sources
Helixi397 – 42327Combined sources
Turni430 – 4345Combined sources
Helixi440 – 45516Combined sources
Helixi458 – 47720Combined sources
Turni478 – 4814Combined sources
Helixi490 – 4978Combined sources
Helixi501 – 51818Combined sources
Helixi523 – 5253Combined sources
Helixi526 – 54823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RM5X-ray2.68A/B2-551[»]
ProteinModelPortaliQ08224.
SMRiQ08224. Positions 2-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the ThiD family.Curated
In the C-terminal section; belongs to the thiaminase-2 family.Curated

Phylogenomic databases

eggNOGiCOG0351.
GeneTreeiENSGT00390000003953.
HOGENOMiHOG000225275.
InParanoidiQ08224.
KOiK00877.
OMAiHIAKESQ.
OrthoDBiEOG75MW5D.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
3.40.1190.20. 1 hit.
InterProiIPR016084. Haem_Oase-like_multi-hlx.
IPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
IPR004305. Thiaminase-2/PQQC.
IPR027574. Thiaminase_II.
[Graphical view]
PfamiPF08543. Phos_pyr_kin. 1 hit.
PF03070. TENA_THI-4. 1 hit.
[Graphical view]
SUPFAMiSSF48613. SSF48613. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
TIGR04306. salvage_TenA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTYSTVSINT PPPYLTLACN EKLPTVLSIA GTDPSGGAGI EADVKTITAH
60 70 80 90 100
RCYAMTCITA LNAQTPVKVY SINNTPKEVV FQTLESNLKD MKCNVIKTGM
110 120 130 140 150
LTAAAIEVLH EKLLQLGENR PKLVVDPVLV ATSGSSLAGK DIVSLITEKV
160 170 180 190 200
APFADILTPN IPECYKLLGE ERKVNGLQDI FQIAKDLAKI TKCSNILVKG
210 220 230 240 250
GHIPWNDEKE KYITDVLFLG AEQKFIIFKG NFVNTTHTHG TGCTLASAIA
260 270 280 290 300
SNLARGYSLP QSVYGGIEYV QNAVAIGCDV TKETVKDNGP INHVYAVEIP
310 320 330 340 350
LEKMLSDECF TASDVIPKKP LKSAADKIPG GNFYEYLINH PKVKPHWDSY
360 370 380 390 400
INHEFVKKVA DGTLERKKFQ FFIEQDYAYL VDYARVHCIA GSKAPCLEDM
410 420 430 440 450
EKELVIVGGV RTEMGQHEKR LKEVFGVKDP DYFQKIKRGP ALRAYSRYFN
460 470 480 490 500
DVSRRGNWQE LVASLTPCLM GYGEALTKMK GKVTAPEGSV YHEWCETYAS
510 520 530 540 550
SWYREAMDEG EKLLNHILET YPPEQLDTLV TIYAEVCELE TNFWTAALEY

E
Length:551
Mass (Da):61,269
Last modified:November 1, 1996 - v1
Checksum:iD57D1C6B693EE401
GO

Sequence cautioni

The sequence CAA62531.1 differs from that shown. Reason: Frameshift at position 544. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti323 – 3231S → G in AAT92799 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62531.1. Frameshift.
Z74797 Genomic DNA. Translation: CAA99063.1.
AY692780 Genomic DNA. Translation: AAT92799.1.
BK006948 Genomic DNA. Translation: DAA10728.1.
PIRiS66740.
RefSeqiNP_014586.1. NM_001183310.1.

Genome annotation databases

EnsemblFungiiYOL055C; YOL055C; YOL055C.
GeneIDi854099.
KEGGisce:YOL055C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91067 Genomic DNA. Translation: CAA62531.1. Frameshift.
Z74797 Genomic DNA. Translation: CAA99063.1.
AY692780 Genomic DNA. Translation: AAT92799.1.
BK006948 Genomic DNA. Translation: DAA10728.1.
PIRiS66740.
RefSeqiNP_014586.1. NM_001183310.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RM5X-ray2.68A/B2-551[»]
ProteinModelPortaliQ08224.
SMRiQ08224. Positions 2-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34346. 17 interactions.
DIPiDIP-8852N.
IntActiQ08224. 1 interaction.

Proteomic databases

MaxQBiQ08224.
PaxDbiQ08224.
PeptideAtlasiQ08224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL055C; YOL055C; YOL055C.
GeneIDi854099.
KEGGisce:YOL055C.

Organism-specific databases

CYGDiYOL055c.
EuPathDBiFungiDB:YOL055C.
SGDiS000005416. THI20.

Phylogenomic databases

eggNOGiCOG0351.
GeneTreeiENSGT00390000003953.
HOGENOMiHOG000225275.
InParanoidiQ08224.
KOiK00877.
OMAiHIAKESQ.
OrthoDBiEOG75MW5D.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00137.
UPA00060; UER00138.
BioCyciMetaCyc:MONOMER3O-77.
YEAST:MONOMER3O-77.
BRENDAi2.7.1.49. 984.
2.7.4.7. 984.
3.5.99.2. 984.

Miscellaneous databases

NextBioi975770.
PROiQ08224.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
3.40.1190.20. 1 hit.
InterProiIPR016084. Haem_Oase-like_multi-hlx.
IPR004399. HMP/HMP-P_kinase.
IPR013749. PM/HMP-P_kinase-1.
IPR029056. Ribokinase-like.
IPR004305. Thiaminase-2/PQQC.
IPR027574. Thiaminase_II.
[Graphical view]
PfamiPF08543. Phos_pyr_kin. 1 hit.
PF03070. TENA_THI-4. 1 hit.
[Graphical view]
SUPFAMiSSF48613. SSF48613. 1 hit.
SSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00097. HMP-P_kinase. 1 hit.
TIGR04306. salvage_TenA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Genetic redundancy and gene fusion in the genome of the Baker's yeast Saccharomyces cerevisiae: functional characterization of a three-member gene family involved in the thiamine biosynthetic pathway."
    Llorente B., Fairhead C., Dujon B.
    Mol. Microbiol. 32:1140-1152(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A HMPP KINASE, INDUCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTHI20_YEAST
AccessioniPrimary (citable) accession number: Q08224
Secondary accession number(s): D6W212, Q05664, Q6B2F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 195 molecules/cell in log phase SD medium.1 Publication

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

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 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.