Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30138 (THIF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfur carrier protein ThiS adenylyltransferase

EC=2.7.7.73
Gene names
Name:thiF
Ordered Locus Names:b3992, JW3956
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + [ThiS] = diphosphate + adenylyl-[ThiS]. Ref.5

Cofactor

Binds 1 zinc ion per subunit. Ref.8 Ref.9

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis.

Subunit structure

Homodimer. Ref.8

Sequence similarities

Belongs to the HesA/MoeB/ThiF family.

Mass spectrometry

Molecular mass is 26970.2 Da from positions 1 - 251. Determined by ESI. Ref.6

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Sulfur carrier protein ThiS adenylyltransferase
PRO_0000120578

Regions

Nucleotide binding127 – 1315ATP
Compositional bias59 – 624Poly-Asp

Sites

Active site1841Glycyl persulfide ester intermediate
Metal binding1691Zinc
Metal binding1721Zinc
Metal binding2401Zinc
Metal binding2431Zinc
Binding site111ATP
Binding site381ATP; via amide nitrogen
Binding site591ATP
Binding site701ATP
Binding site831ATP
Binding site1071ATP; via amide nitrogen

Amino acid modifications

Cross-link184Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS)

Experimental info

Mutagenesis1741W → A: No adenylation of ThiS. Ref.8
Mutagenesis1841C → S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth. Ref.7
Sequence conflict229 – 2302WR → C in AAB95618. Ref.1

Secondary structure

............................................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30138 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 9CB9E20FD094F12D

FASTA25126,970
        10         20         30         40         50         60 
MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA GVGTLVLADD 

        70         80         90        100        110        120 
DDVHLSNLQR QILFTTEDID RPKSQVSQQR LTQLNPDIQL TALQQRLTGE ALKDAVARAD 

       130        140        150        160        170        180 
VVLDCTDNMA TRQEINAACV ALNTPLITAS AVGFGGQLMV LTPPWEQGCY RCLWPDNQEP 

       190        200        210        220        230        240 
ERNCRTAGVV GPVVGVMGTL QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRASGC 

       250 
PVCGGSNADP V 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Structural analysis of Escherichia coli ThiF."
Duda D.M., Walden H., Sfondouris J., Schulman B.A.
J. Mol. Biol. 349:774-786(2005) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRC65206.
RefSeqNP_418420.4. NC_000913.3.
YP_491468.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZFNX-ray2.75A/B/C/D1-251[»]
1ZKMX-ray2.95A/B/C/D1-251[»]
1ZUDX-ray1.981/31-251[»]
ProteinModelPortalP30138.
SMRP30138. Positions 1-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP30138. 8 interactions.
STRING511145.b3992.

Proteomic databases

PaxDbP30138.
PRIDEP30138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76966; AAC76966; b3992.
BAE77327; BAE77327; BAE77327.
GeneID12933663.
948500.
KEGGecj:Y75_p3204.
eco:b3992.
PATRIC32123507. VBIEscCol129921_4106.

Organism-specific databases

EchoBASEEB1546.
EcoGeneEG11587. thiF.

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000281217.
KOK03148.
OMAGCYACLY.
OrthoDBEOG628F8J.
PhylomeDBP30138.
ProtClustDBCLSK889561.

Enzyme and pathway databases

BioCycEcoCyc:THIF-MONOMER.
ECOL316407:JW3956-MONOMER.
MetaCyc:THIF-MONOMER.
UniPathwayUPA00060.

Gene expression databases

GenevestigatorP30138.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR012731. Adenyl_ThiF.
IPR007901. MoeZ_MoeB.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamPF05237. MoeZ_MoeB. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 1 hit.
TIGRFAMsTIGR02356. adenyl_thiF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP30138.
PROP30138.

Entry information

Entry nameTHIF_ECOLI
AccessionPrimary (citable) accession number: P30138
Secondary accession number(s): P76780, Q2M8S9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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