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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 6611 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661H → N or G: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3393394-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthasePRO_0000431581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621N6-(pyridoxal phosphate)lysine1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi11 – 144Combined sources
Helixi16 – 183Combined sources
Helixi19 – 268Combined sources
Helixi29 – 324Combined sources
Beta strandi36 – 449Combined sources
Helixi45 – 473Combined sources
Helixi48 – 536Combined sources
Beta strandi56 – 638Combined sources
Helixi64 – 729Combined sources
Beta strandi77 – 848Combined sources
Beta strandi89 – 946Combined sources
Helixi103 – 1064Combined sources
Beta strandi110 – 1167Combined sources
Helixi117 – 12610Combined sources
Helixi127 – 1293Combined sources
Helixi133 – 1353Combined sources
Beta strandi136 – 1405Combined sources
Helixi142 – 1443Combined sources
Helixi145 – 1506Combined sources
Beta strandi153 – 1608Combined sources
Turni161 – 1633Combined sources
Helixi164 – 17411Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1865Combined sources
Helixi187 – 1904Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2066Combined sources
Helixi207 – 2126Combined sources
Helixi214 – 23320Combined sources
Helixi235 – 24511Combined sources
Helixi247 – 2504Combined sources
Helixi252 – 26211Combined sources
Helixi273 – 28513Combined sources
Helixi313 – 33018Combined sources

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 1184Pyridoxal phosphate binding1 Publication

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi195 – 1995CCCFC; essential for catalytic activity, may be the site of iron coordinationBy similarity

Sequence similaritiesi

Belongs to the NMT1/THI5 family.Curated

Phylogenomic databases

HOGENOMiHOG000160891.
OMAiCCFCTIL.
OrthoDBiEOG7DRJD1.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4ESWX-ray1.60A/B1-339[»]
4ESXX-ray2.20A/B1-339[»]
ProteinModelPortaliC4YMW2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEEQ43943; EEQ43943; CAWG_02199.

Phylogenomic databases

HOGENOMiHOG000160891.
OMAiCCFCTIL.
OrthoDBiEOG7DRJD1.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WO-1.
  2. "Thiamin pyrimidine biosynthesis in Candida albicans: a remarkable reaction between histidine and pyridoxal phosphate."
    Lai R.Y., Huang S., Fenwick M.K., Hazra A., Zhang Y., Rajashankar K., Philmus B., Kinsland C., Sanders J.M., Ealick S.E., Begley T.P.
    J. Am. Chem. Soc. 134:9157-9159(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND OF MUTANT GLY-66, FUNCTION, ACTIVE SITE, COFACTOR, SUBUNIT, MASS SPECTROMETRY, MUTAGENESIS OF HIS-66.

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 11, 2015
This is version 31 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.