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Protein

Thiamine thiazole synthase

Gene

thi2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei87 – 871Substrate; via amide nitrogenUniRule annotation
Binding sitei116 – 1161Substrate; via amide nitrogenUniRule annotation
Binding sitei181 – 1811Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei217 – 2171SubstrateUniRule annotation
Binding sitei232 – 2321SubstrateUniRule annotation
Binding sitei284 – 2841Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • response to stress Source: InterPro
  • thiamine biosynthetic process Source: PomBase
  • thiazole biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

Iron, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine thiazole synthaseUniRule annotation
Alternative name(s):
Thiazole biosynthetic enzymeUniRule annotation
Gene namesi
Name:thi2
Synonyms:nmt2
ORF Names:SPBC26H8.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC26H8.01.
PomBaseiSPBC26H8.01. thi2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Thiamine thiazole synthasePRO_0000034056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 21512,3-didehydroalanine (Cys)UniRule annotation

Post-translational modificationi

During the catalytic reaction, a sulfide is transferred from Cys-215 to a reaction intermediate, generating a dehydroalanine residue.UniRule annotation

Expressioni

Inductioni

Repressed by thiamine.1 Publication

Interactioni

Subunit structurei

Homooctamer.UniRule annotation

Protein-protein interaction databases

BioGridi277054. 6 interactions.
MINTiMINT-4689959.

Structurei

3D structure databases

ProteinModelPortaliP40998.
SMRiP40998. Positions 48-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1092Substrate bindingUniRule annotation
Regioni294 – 2963Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the THI4 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000106048.
InParanoidiP40998.
KOiK03146.
OMAiRMGPVFG.
OrthoDBiEOG7ZKSN0.
PhylomeDBiP40998.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_03158. THI4.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR027495. Sti35.
IPR002922. Thi4_fam.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00292. TIGR00292. 1 hit.

Sequencei

Sequence statusi: Complete.

P40998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPATAVVTP QTAFKTDLPV EKTAHNTVVK SEMGALSKAY PTYSLDESFS
60 70 80 90 100
FAPIRESTVS RAMTRRYFSD LDKYAESDIV IVGAGSAGLT AAYYIGTRRP
110 120 130 140 150
DLKIAIIEAS VAPGGGAWLG GQLFSAMVVR KPADLFLNEI GVPYEDEGDY
160 170 180 190 200
VVVKHAALFT STVMARTLAL PNVKLFNATA VEDLIVKEGK DGKQRIAGVV
210 220 230 240 250
TNWTLVSLNH GLQSCMDPNT INAHLVVSAT GHDGPFGAFC VKRLASAQLV
260 270 280 290 300
SNLHDMRPLD MNRAEDLIVK GTREVFPGMI VGGMELSEFD GANRMGPTFG
310 320
GMMFSGIKAA QEALAIFDER KAVNEKYL
Length:328
Mass (Da):35,274
Last modified:January 11, 2001 - v2
Checksum:iBF18CCB367BEC421
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti299 – 32830FGGMM…NEKYL → SVV in CAA57779 (PubMed:7992507).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82363 Genomic DNA. Translation: CAA57779.1.
CU329671 Genomic DNA. Translation: CAA21093.1.
PIRiT40013.
RefSeqiNP_596642.1. NM_001022564.2.

Genome annotation databases

EnsemblFungiiSPBC26H8.01.1; SPBC26H8.01.1:pep; SPBC26H8.01.
GeneIDi2540526.
KEGGispo:SPBC26H8.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82363 Genomic DNA. Translation: CAA57779.1.
CU329671 Genomic DNA. Translation: CAA21093.1.
PIRiT40013.
RefSeqiNP_596642.1. NM_001022564.2.

3D structure databases

ProteinModelPortaliP40998.
SMRiP40998. Positions 48-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277054. 6 interactions.
MINTiMINT-4689959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC26H8.01.1; SPBC26H8.01.1:pep; SPBC26H8.01.
GeneIDi2540526.
KEGGispo:SPBC26H8.01.

Organism-specific databases

EuPathDBiFungiDB:SPBC26H8.01.
PomBaseiSPBC26H8.01. thi2.

Phylogenomic databases

HOGENOMiHOG000106048.
InParanoidiP40998.
KOiK03146.
OMAiRMGPVFG.
OrthoDBiEOG7ZKSN0.
PhylomeDBiP40998.

Miscellaneous databases

PROiP40998.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_03158. THI4.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR027495. Sti35.
IPR002922. Thi4_fam.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00292. TIGR00292. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "nmt2 of fission yeast: a second thiamine-repressible gene co-ordinately regulated with nmt1."
    Manetti A.G.O., Rosetto M., Maundrell K.G.
    Yeast 10:1075-1082(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTHI4_SCHPO
AccessioniPrimary (citable) accession number: P40998
Secondary accession number(s): O74785
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 11, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.