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Protein

Thiamine thiazole synthase

Gene

thi4

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.2 Publications

Miscellaneous

Unlike THI4 from S.cerevisiae, Thi4 from M.jannaschii can catalyze multiple turnovers because the sulfide is not enzyme derived.1 Publication

Cofactori

Fe2+2 PublicationsNote: Binds 1 Fe2+ ion per subunit. Other divalent metal cations can support activity.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
Binding sitei47NAD1 Publication1
Binding sitei74NAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei138NAD; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi166Iron; shared with adjacent protomerUniRule annotation1
Metal bindingi181IronUniRule annotation1
Binding sitei184NAD; via carbonyl oxygen1 Publication1
Binding sitei230NAD; via amide nitrogen1 Publication1
Binding sitei240GlycineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 67NAD1 Publication2
Nucleotide bindingi164 – 166NAD; shared with adjacent protomer1 Publication3

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • lyase activity Source: UniProtKB-KW
  • oxidoreductase activity Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processThiamine biosynthesis
LigandIron, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine thiazole synthase1 Publication (EC:4.-.-.-2 Publications)
Gene namesi
Name:thi41 Publication
Ordered Locus Names:MJ0601
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi164H → C: Still requires free sulfide for ADT synthesis, showing that this cysteine cannot act as an enzyme-derived sulfur source for thiazole formation as in S.cerevisiae. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001539471 – 267Thiamine thiazole synthaseAdd BLAST267

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0601.

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 34Combined sources19
Beta strandi36 – 42Combined sources7
Helixi46 – 57Combined sources12
Beta strandi62 – 70Combined sources9
Turni74 – 78Combined sources5
Beta strandi82 – 88Combined sources7
Turni89 – 92Combined sources4
Helixi93 – 96Combined sources4
Turni97 – 99Combined sources3
Beta strandi103 – 106Combined sources4
Beta strandi109 – 113Combined sources5
Helixi116 – 127Combined sources12
Beta strandi131 – 144Combined sources14
Beta strandi147 – 155Combined sources9
Helixi156 – 161Combined sources6
Beta strandi168 – 177Combined sources10
Helixi180 – 182Combined sources3
Helixi184 – 192Combined sources9
Helixi207 – 217Combined sources11
Beta strandi219 – 222Combined sources4
Beta strandi225 – 227Combined sources3
Helixi230 – 235Combined sources6
Helixi246 – 263Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Y4MX-ray2.71A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ58018.
SMRiQ58018.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the THI4 family.Curated

Phylogenomic databases

eggNOGiarCOG00574. Archaea.
COG1635. LUCA.
InParanoidiQ58018.
KOiK03146.
OrthoDBiPOG093Z09PU.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00304. Thi4. 1 hit.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR002922. Thi4_fam.
IPR022828. Thi4_putative.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00292. TIGR00292. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNLMNIKDI KLNADETKTT KAILKASFDM WLDIVEADVV IVGAGPSGLT
60 70 80 90 100
CARYLAKEGF KVVVLERHLA FGGGTWGGGM GFPYIVVEEP ADELLREVGI
110 120 130 140 150
KLIDMGDGYY VADSVEVPAK LAVAAMDAGA KILTGIVVED LILREDGVAG
160 170 180 190 200
VVINSYAIER AGLHIDPLTI RSKVVVDATG HEASIVNILV KKNKLEADVP
210 220 230 240 250
GEKSMWAEKG ENALLRNTRE VYPNLFVCGM AANASHGGYR MGAIFGGMYL
260
SGKLCAELIT EKLKNKE
Length:267
Mass (Da):28,655
Last modified:November 2, 2010 - v3
Checksum:i2F359B900C838251
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98592.1.
PIRiA64375.

Genome annotation databases

EnsemblBacteriaiAAB98592; AAB98592; MJ_0601.
KEGGimja:MJ_0601.

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.

Entry informationi

Entry nameiTHI4_METJA
AccessioniPrimary (citable) accession number: Q58018
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: July 5, 2017
This is version 105 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

This protein was originally thought to have NAD-dependent ribose 1,5-bisphosphate isomerase activity but the recombinant protein was not active in vitro (PubMed:15375115, PubMed:26919468). In contrast, another protein from M.jannaschii likely possesses this activity (MJ0122).2 Publications

Keywords - Technical termi

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

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families