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P30138

- THIF_ECOLI

UniProt

P30138 - THIF_ECOLI

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP30138.
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

        10         20         30         40         50
MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA
60 70 80 90 100
GVGTLVLADD DDVHLSNLQR QILFTTEDID RPKSQVSQQR LTQLNPDIQL
110 120 130 140 150
TALQQRLTGE ALKDAVARAD VVLDCTDNMA TRQEINAACV ALNTPLITAS
160 170 180 190 200
AVGFGGQLMV LTPPWEQGCY RCLWPDNQEP ERNCRTAGVV GPVVGVMGTL
210 220 230 240 250
QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRASGC PVCGGSNADP

V
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.
InParanoidi P30138.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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