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P30138

- THIF_ECOLI

UniProt

P30138 - THIF_ECOLI

Protein

Sulfur carrier protein ThiS adenylyltransferase

Gene

thiF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS.

    Catalytic activityi

    ATP + [ThiS] = diphosphate + adenylyl-[ThiS].1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111ATP
    Binding sitei38 – 381ATP; via amide nitrogen
    Binding sitei59 – 591ATP
    Binding sitei70 – 701ATP
    Binding sitei83 – 831ATP
    Binding sitei107 – 1071ATP; via amide nitrogen
    Metal bindingi169 – 1691Zinc1 Publication
    Metal bindingi172 – 1721Zinc1 Publication
    Active sitei184 – 1841Glycyl persulfide ester intermediate
    Metal bindingi240 – 2401Zinc1 Publication
    Metal bindingi243 – 2431Zinc1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi127 – 1315ATP

    GO - Molecular functioni

    1. ATP binding Source: EcoCyc
    2. magnesium ion binding Source: EcoCyc
    3. metal ion binding Source: EcoCyc
    4. nucleotidyltransferase activity Source: EcoCyc
    5. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. cellular protein modification process Source: RefGenome
    2. thiamine biosynthetic process Source: UniProtKB-KW
    3. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Thiamine biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:THIF-MONOMER.
    ECOL316407:JW3956-MONOMER.
    MetaCyc:THIF-MONOMER.
    UniPathwayiUPA00060.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfur carrier protein ThiS adenylyltransferase (EC:2.7.7.73)
    Gene namesi
    Name:thiF
    Ordered Locus Names:b3992, JW3956
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11587. thiF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi174 – 1741W → A: No adenylation of ThiS. 1 Publication
    Mutagenesisi184 – 1841C → S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Sulfur carrier protein ThiS adenylyltransferasePRO_0000120578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki184 – 184Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS)

    Keywords - PTMi

    Thioester bond

    Proteomic databases

    PaxDbiP30138.
    PRIDEiP30138.

    Expressioni

    Gene expression databases

    GenevestigatoriP30138.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    IntActiP30138. 8 interactions.
    STRINGi511145.b3992.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 86
    Helixi10 – 134
    Turni16 – 183
    Helixi19 – 279
    Beta strandi30 – 345
    Helixi40 – 4910
    Beta strandi53 – 586
    Helixi65 – 673
    Turni68 – 703
    Helixi76 – 783
    Helixi83 – 9412
    Beta strandi98 – 1036
    Helixi109 – 11810
    Beta strandi120 – 1245
    Helixi129 – 14113
    Beta strandi146 – 1538
    Beta strandi155 – 1617
    Helixi170 – 1734
    Beta strandi176 – 1783
    Helixi191 – 21020
    Beta strandi217 – 2237
    Turni224 – 2274
    Beta strandi228 – 2336
    Turni241 – 2433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZFNX-ray2.75A/B/C/D1-251[»]
    1ZKMX-ray2.95A/B/C/D1-251[»]
    1ZUDX-ray1.981/31-251[»]
    ProteinModelPortaliP30138.
    SMRiP30138. Positions 1-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30138.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi59 – 624Poly-Asp

    Sequence similaritiesi

    Belongs to the HesA/MoeB/ThiF family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000281217.
    KOiK03148.
    OMAiCTDNMST.
    OrthoDBiEOG628F8J.
    PhylomeDBiP30138.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR012731. Adenyl_ThiF.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PfamiPF05237. MoeZ_MoeB. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.
    TIGRFAMsiTIGR02356. adenyl_thiF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P30138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA    50
    GVGTLVLADD DDVHLSNLQR QILFTTEDID RPKSQVSQQR LTQLNPDIQL 100
    TALQQRLTGE ALKDAVARAD VVLDCTDNMA TRQEINAACV ALNTPLITAS 150
    AVGFGGQLMV LTPPWEQGCY RCLWPDNQEP ERNCRTAGVV GPVVGVMGTL 200
    QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRASGC PVCGGSNADP 250
    V 251
    Length:251
    Mass (Da):26,970
    Last modified:October 1, 1993 - v2
    Checksum:i9CB9E20FD094F12D
    GO

    Sequence cautioni

    The sequence AAC43090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2302WR → C in AAB95618. (PubMed:8432721)Curated

    Mass spectrometryi

    Molecular mass is 26970.2 Da from positions 1 - 251. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88701 Genomic DNA. Translation: AAB95618.1.
    U00006 Genomic DNA. Translation: AAC43090.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76966.2.
    AP009048 Genomic DNA. Translation: BAE77327.1.
    PIRiC65206.
    RefSeqiNP_418420.4. NC_000913.3.
    YP_491468.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76966; AAC76966; b3992.
    BAE77327; BAE77327; BAE77327.
    GeneIDi12933663.
    948500.
    KEGGiecj:Y75_p3204.
    eco:b3992.
    PATRICi32123507. VBIEscCol129921_4106.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88701 Genomic DNA. Translation: AAB95618.1 .
    U00006 Genomic DNA. Translation: AAC43090.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC76966.2 .
    AP009048 Genomic DNA. Translation: BAE77327.1 .
    PIRi C65206.
    RefSeqi NP_418420.4. NC_000913.3.
    YP_491468.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZFN X-ray 2.75 A/B/C/D 1-251 [» ]
    1ZKM X-ray 2.95 A/B/C/D 1-251 [» ]
    1ZUD X-ray 1.98 1/3 1-251 [» ]
    ProteinModelPortali P30138.
    SMRi P30138. Positions 1-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P30138. 8 interactions.
    STRINGi 511145.b3992.

    Proteomic databases

    PaxDbi P30138.
    PRIDEi P30138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76966 ; AAC76966 ; b3992 .
    BAE77327 ; BAE77327 ; BAE77327 .
    GeneIDi 12933663.
    948500.
    KEGGi ecj:Y75_p3204.
    eco:b3992.
    PATRICi 32123507. VBIEscCol129921_4106.

    Organism-specific databases

    EchoBASEi EB1546.
    EcoGenei EG11587. thiF.

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000281217.
    KOi K03148.
    OMAi CTDNMST.
    OrthoDBi EOG628F8J.
    PhylomeDBi P30138.

    Enzyme and pathway databases

    UniPathwayi UPA00060 .
    BioCyci EcoCyc:THIF-MONOMER.
    ECOL316407:JW3956-MONOMER.
    MetaCyc:THIF-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P30138.
    PROi P30138.

    Gene expression databases

    Genevestigatori P30138.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR012731. Adenyl_ThiF.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    Pfami PF05237. MoeZ_MoeB. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    TIGRFAMsi TIGR02356. adenyl_thiF. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12."
      Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.
      J. Bacteriol. 175:982-992(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation."
      Taylor S.V., Kelleher N.L., Kinsland C., Chiu H.-J., Costello C.A., Backstrom A.D., McLafferty F.W., Begley T.P.
      J. Biol. Chem. 273:16555-16560(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, REACTION PRODUCT.
      Strain: B/r / ATCC 12407.
    6. "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry."
      Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W.
      Protein Sci. 7:1796-1801(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
    7. "Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex."
      Xi J., Ge Y., Kinsland C., McLafferty F.W., Begley T.P.
      Proc. Natl. Acad. Sci. U.S.A. 98:8513-8518(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO SULFUR CARRIER PROTEIN THIS, MUTAGENESIS OF CYS-184, REACTION MECHANISM.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEXES WITH ZINC WITH OR WITOUT ATP, COFACTOR, SUBUNIT, MUTAGENESIS OF TRP-174.
    9. "Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis."
      Lehmann C., Begley T.P., Ealick S.E.
      Biochemistry 45:11-19(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH ZINC AND SULFUR CARRIER PROTEIN THIS, COFACTOR, REACTION MECHANISM.

    Entry informationi

    Entry nameiTHIF_ECOLI
    AccessioniPrimary (citable) accession number: P30138
    Secondary accession number(s): P76780, Q2M8S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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

    External Data

    Dasty 3