Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiamine thiazole synthase

Gene

NCU06110

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.UniRule annotation1 Publication

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei90Substrate; via amide nitrogen1
Binding sitei119Substrate; via amide nitrogen1
Binding sitei184Substrate; via amide nitrogen and carbonyl oxygen1
Binding sitei234Substrate1
Binding sitei249Substrate1
Binding sitei301Substrate; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processThiamine biosynthesis
LigandIron, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine thiazole synthaseUniRule annotation
Alternative name(s):
37 kDa NcCyP41-binding protein
Short name:
CyPBP37
Thiazole biosynthetic enzymeUniRule annotation
Gene namesi
ORF Names:NCU06110
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 7, Linkage Group VII

Organism-specific databases

EuPathDBiFungiDB:NCU06110

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004158771 – 344Thiamine thiazole synthaseAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2322,3-didehydroalanine (Cys)UniRule annotation1

Post-translational modificationi

During the catalytic reaction, a sulfide is transferred from Cys-232 to a reaction intermediate, generating a dehydroalanine residue.UniRule annotation

Proteomic databases

PRIDEiQ1K6I4

Expressioni

Inductioni

Repressed by thiamine, but not by thiazole. Induced by various stress conditions, including heat, cold or osmotic shock.1 Publication

Interactioni

Subunit structurei

Homooctamer (By similarity). Interacts with cyp-41.UniRule annotation2 Publications

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 43Combined sources6
Helixi44 – 46Combined sources3
Helixi59 – 78Combined sources20
Beta strandi81 – 85Combined sources5
Helixi89 – 101Combined sources13
Beta strandi107 – 115Combined sources9
Turni118 – 121Combined sources4
Beta strandi130 – 133Combined sources4
Turni134 – 136Combined sources3
Helixi137 – 143Combined sources7
Beta strandi151 – 157Combined sources7
Helixi159 – 171Combined sources13
Beta strandi176 – 180Combined sources5
Beta strandi182 – 191Combined sources10
Beta strandi211 – 220Combined sources10
Helixi221 – 224Combined sources4
Beta strandi227 – 229Combined sources3
Beta strandi236 – 239Combined sources4
Beta strandi241 – 245Combined sources5
Beta strandi249 – 254Combined sources6
Helixi256 – 263Combined sources8
Beta strandi266 – 268Combined sources3
Beta strandi274 – 276Combined sources3
Helixi278 – 287Combined sources10
Beta strandi290 – 293Combined sources4
Beta strandi296 – 298Combined sources3
Helixi300 – 302Combined sources3
Helixi303 – 307Combined sources5
Helixi317 – 341Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JSKX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-344[»]
ProteinModelPortaliQ1K6I4
SMRiQ1K6I4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 112Substrate binding2
Regioni311 – 313Substrate binding3

Sequence similaritiesi

Belongs to the THI4 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000106048
InParanoidiQ1K6I4
KOiK03146
OMAiMWGGGMM
OrthoDBiEOG092C3CAV

Family and domain databases

Gene3Di3.50.50.60, 1 hit
HAMAPiMF_03158 THI4, 1 hit
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR027495 Sti35
IPR002922 Thi4_fam
SUPFAMiSSF51905 SSF51905, 1 hit
TIGRFAMsiTIGR00292 TIGR00292, 1 hit

Sequencei

Sequence statusi: Complete.

Q1K6I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPSVLEPQS VPTLVNVGLK AVGRNDAPVE RDARGLSKPL LELMPTLGTD
60 70 80 90 100
AFTFSPIRES TVSRAMTRRY FADLDAHAET DIVIVGAGSC GLSAAYVLST
110 120 130 140 150
LRPDLRITIV EAGVAPGGGA WLGGQLFSAM VMRKPADVFL DEVGVPYEDE
160 170 180 190 200
GDYVVVKHAA LFTSTVLSKV LQRPNVKLFN ATTVEDLITR KHHAESSSSS
210 220 230 240 250
DDGEAEDEAK VRIAGVVTNW TLVSMHHDDQ SCMDPNTINA PVIISTTGHD
260 270 280 290 300
GPFGAFSVKR LVSMKQMERL NGMRGLDMQS AEDAIVNNTR EIVPGLIVGG
310 320 330 340
MELSEIDGAN RMGPTFGAMA LSGVKAAHEA IRVFDLRKAQ NDKC
Length:344
Mass (Da):36,864
Last modified:June 28, 2011 - v1
Checksum:iAF9721DCEB155E64
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31R → RV AA sequence (PubMed:14568539).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ297565 mRNA Translation: CAC03570.1
CM002242 Genomic DNA Translation: ESA41902.1
CM002242 Genomic DNA Translation: ESA41903.1
CM002242 Genomic DNA Translation: ESA41904.1
CM002242 Genomic DNA Translation: ESA41905.1
RefSeqiXP_011395239.1, XM_011396937.1
XP_011395240.1, XM_011396938.1
XP_011395241.1, XM_011396939.1
XP_011395242.1, XM_011396940.1

Genome annotation databases

EnsemblFungiiESA41902; ESA41902; NCU06110
ESA41903; ESA41903; NCU06110
ESA41904; ESA41904; NCU06110
ESA41905; ESA41905; NCU06110
GeneIDi3876110
KEGGincr:NCU06110

Similar proteinsi

Entry informationi

Entry nameiTHI4_NEUCR
AccessioniPrimary (citable) accession number: Q1K6I4
Secondary accession number(s): Q9HGR2, V5IKI8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: June 28, 2011
Last modified: May 23, 2018
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health