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Protein

Sulfur carrier protein ThiS adenylyltransferase

Gene

thiF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.
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 sitei11ATP1
Binding sitei38ATP; via amide nitrogen1
Binding sitei59ATP1
Binding sitei70ATP1
Binding sitei83ATP1
Binding sitei107ATP; via amide nitrogen1
Metal bindingi169Zinc1 Publication1
Metal bindingi172Zinc1 Publication1
Active sitei184Glycyl persulfide ester intermediate1
Metal bindingi240Zinc1 Publication1
Metal bindingi243Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 131ATP5

GO - Molecular functioni

  • ATP binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • metal ion binding Source: EcoCyc
  • nucleotidyltransferase activity Source: EcoCyc
  • small protein activating enzyme activity Source: InterPro
  • zinc ion binding Source: EcoCyc

GO - Biological processi

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.
BRENDAi2.7.7.73. 2026.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11587. thiF.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi174W → A: No adenylation of ThiS. 1 Publication1
Mutagenesisi184C → S: No cross-link formed with ThiS. No effect on ThiS thiocarboxylate formation in vitro. Does not support growth. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001205781 – 251Sulfur carrier protein ThiS adenylyltransferaseAdd BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki184Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS)

Keywords - PTMi

Thioester bond

Proteomic databases

EPDiP30138.
PaxDbiP30138.
PRIDEiP30138.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4262657. 10 interactors.
IntActiP30138. 8 interactors.
STRINGi511145.b3992.

Structurei

Secondary structure

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Helixi10 – 13Combined sources4
Turni16 – 18Combined sources3
Helixi19 – 27Combined sources9
Beta strandi30 – 34Combined sources5
Helixi40 – 49Combined sources10
Beta strandi53 – 58Combined sources6
Helixi65 – 67Combined sources3
Turni68 – 70Combined sources3
Helixi76 – 78Combined sources3
Helixi83 – 94Combined sources12
Beta strandi98 – 103Combined sources6
Helixi109 – 118Combined sources10
Beta strandi120 – 124Combined sources5
Helixi129 – 141Combined sources13
Beta strandi146 – 153Combined sources8
Beta strandi155 – 161Combined sources7
Helixi170 – 173Combined sources4
Beta strandi176 – 178Combined sources3
Helixi191 – 210Combined sources20
Beta strandi217 – 223Combined sources7
Turni224 – 227Combined sources4
Beta strandi228 – 233Combined sources6
Turni241 – 243Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP30138.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi59 – 62Poly-Asp4

Sequence similaritiesi

Belongs to the HesA/MoeB/ThiF family.Curated

Phylogenomic databases

eggNOGiENOG4105D06. Bacteria.
COG0476. LUCA.
HOGENOMiHOG000281217.
InParanoidiP30138.
KOiK03148.
OMAiYHCLFPF.
PhylomeDBiP30138.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012731. Adenyl_ThiF.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti229 – 230WR → C in AAB95618 (PubMed:8432721).Curated2

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000999737.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76966; AAC76966; b3992.
BAE77327; BAE77327; BAE77327.
GeneIDi948500.
KEGGiecj:JW3956.
eco:b3992.
PATRICi32123507. VBIEscCol129921_4106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000999737.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4262657. 10 interactors.
IntActiP30138. 8 interactors.
STRINGi511145.b3992.

Proteomic databases

EPDiP30138.
PaxDbiP30138.
PRIDEiP30138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76966; AAC76966; b3992.
BAE77327; BAE77327; BAE77327.
GeneIDi948500.
KEGGiecj:JW3956.
eco:b3992.
PATRICi32123507. VBIEscCol129921_4106.

Organism-specific databases

EchoBASEiEB1546.
EcoGeneiEG11587. thiF.

Phylogenomic databases

eggNOGiENOG4105D06. Bacteria.
COG0476. LUCA.
HOGENOMiHOG000281217.
InParanoidiP30138.
KOiK03148.
OMAiYHCLFPF.
PhylomeDBiP30138.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciEcoCyc:THIF-MONOMER.
ECOL316407:JW3956-MONOMER.
MetaCyc:THIF-MONOMER.
BRENDAi2.7.7.73. 2026.

Miscellaneous databases

EvolutionaryTraceiP30138.
PROiP30138.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012731. Adenyl_ThiF.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR02356. adenyl_thiF. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 137 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

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.