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Protein

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

Gene

THI5

Organism
Candida albicans (strain WO-1) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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

Fe3+1 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

Complete GO annotation...

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Iron, Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthaseBy similarity
Short name:
HMP-P synthaseCurated
Short name:
Hydroxymethylpyrimidine phosphate synthaseCurated
Alternative name(s):
Thiamine biosynthesis protein 51 Publication
Thiamine pyrimidine synthase1 Publication
Gene namesi
Name:THI51 Publication
ORF Names:CAWG_02199
OrganismiCandida albicans (strain WO-1) (Yeast)
Taxonomic identifieri294748 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000001429 Componenti: Chromosome R

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi66H → N or G: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004315811 – 3394-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthaseAdd BLAST339

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi11 – 14Combined sources4
Helixi16 – 18Combined sources3
Helixi19 – 26Combined sources8
Helixi29 – 32Combined sources4
Beta strandi36 – 44Combined sources9
Helixi45 – 47Combined sources3
Helixi48 – 53Combined sources6
Beta strandi56 – 63Combined sources8
Helixi64 – 72Combined sources9
Beta strandi77 – 84Combined sources8
Beta strandi89 – 94Combined sources6
Helixi103 – 106Combined sources4
Beta strandi110 – 116Combined sources7
Helixi117 – 126Combined sources10
Helixi127 – 129Combined sources3
Helixi133 – 135Combined sources3
Beta strandi136 – 140Combined sources5
Helixi142 – 144Combined sources3
Helixi145 – 150Combined sources6
Beta strandi153 – 160Combined sources8
Turni161 – 163Combined sources3
Helixi164 – 174Combined sources11
Helixi179 – 181Combined sources3
Beta strandi182 – 186Combined sources5
Helixi187 – 190Combined sources4
Helixi197 – 199Combined sources3
Beta strandi201 – 206Combined sources6
Helixi207 – 212Combined sources6
Helixi214 – 233Combined sources20
Helixi235 – 245Combined sources11
Helixi247 – 250Combined sources4
Helixi252 – 262Combined sources11
Helixi273 – 285Combined sources13
Helixi313 – 330Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ESWX-ray1.60A/B1-339[»]
4ESXX-ray2.20A/B1-339[»]
ProteinModelPortaliC4YMW2.
SMRiC4YMW2.
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 coordinationBy similarity5

Sequence similaritiesi

Belongs to the NMT1/THI5 family.Curated

Phylogenomic databases

HOGENOMiHOG000160891.
OMAiCCFCTIL.
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.

C4YMW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNKITFLL NWEAAPYHIP VYLANIKGYF KDENLDIAIL EPSNPSDVTE
60 70 80 90 100
LVGSGKVDMG LKAMVHTLAA KARGFPVTSI GSLLDEPFTG ICYLEGSGIT
110 120 130 140 150
SDFQSLKGKR IGYVGEFGKI QVDELTKHYG MTPDDYVAVR CGMNVAKYIL
160 170 180 190 200
EGTIDCGIGI ECIQQVELEE ALKEQGKDSN DAKMLRIDKL AELGCCCFCT
210 220 230 240 250
ILYIANDKFI AENPQAVKKF LKAIKRATDY MLAHPREAWA EYGNFKPTMQ
260 270 280 290 300
TDLNTKKFQR CYAYFSESLY NVHRDWRKVN NYGKRLDILP ENYVPNYTNE
310 320 330
YLSWPEPKEV DDPEKAQDLM LKHQEECKTC GGYKRLVLA
Length:339
Mass (Da):38,377
Last modified:July 28, 2009 - v1
Checksum:iA9E0369CC337659F
GO

Mass spectrometryi

Molecular mass is 40408 Da from positions 1 - 339. Determined by ESI. The measured mass includes the mass of an N-terminal poly-histidine tag, expressed in E.coli.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000309 Genomic DNA. Translation: EEQ43943.1.

Genome annotation databases

EnsemblFungiiEEQ43943; EEQ43943; CAWG_02199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000309 Genomic DNA. Translation: EEQ43943.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ESWX-ray1.60A/B1-339[»]
4ESXX-ray2.20A/B1-339[»]
ProteinModelPortaliC4YMW2.
SMRiC4YMW2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEEQ43943; EEQ43943; CAWG_02199.

Phylogenomic databases

HOGENOMiHOG000160891.
OMAiCCFCTIL.
OrthoDBiEOG092C349S.

Enzyme and pathway databases

UniPathwayiUPA00060.

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_CANAW
AccessioniPrimary (citable) accession number: C4YMW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 7, 2015
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 33 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

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

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.