THIF_ECOLI
ID THIF_ECOLI Reviewed; 251 AA.
AC P30138; P76780; Q2M8S9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Sulfur carrier protein ThiS adenylyltransferase;
DE EC=2.7.7.73;
GN Name=thiF; OrderedLocusNames=b3992, JW3956;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT Escherichia coli K-12.";
RL J. Bacteriol. 175:982-992(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CATALYTIC ACTIVITY, AND REACTION PRODUCT.
RC STRAIN=B/r / ATCC 12407;
RX PubMed=9632726; DOI=10.1074/jbc.273.26.16555;
RA Taylor S.V., Kelleher N.L., Kinsland C., Chiu H.-J., Costello C.A.,
RA Backstrom A.D., McLafferty F.W., Begley T.P.;
RT "Thiamin biosynthesis in Escherichia coli. Identification of ThiS
RT thiocarboxylate as the immediate sulfur donor in the thiazole formation.";
RL J. Biol. Chem. 273:16555-16560(1998).
RN [6]
RP MASS SPECTROMETRY.
RX PubMed=10082377; DOI=10.1002/pro.5560070815;
RA Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J.,
RA Begley T.P., McLafferty F.W.;
RT "Efficient sequence analysis of the six gene products (7-74 kDa) from the
RT Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass
RT spectrometry.";
RL Protein Sci. 7:1796-1801(1998).
RN [7]
RP CROSS-LINKING TO SULFUR CARRIER PROTEIN THIS, MUTAGENESIS OF CYS-184, AND
RP REACTION MECHANISM.
RX PubMed=11438688; DOI=10.1073/pnas.141226698;
RA Xi J., Ge Y., Kinsland C., McLafferty F.W., Begley T.P.;
RT "Biosynthesis of the thiazole moiety of thiamin in Escherichia coli:
RT identification of an acyldisulfide-linked protein--protein conjugate that
RT is functionally analogous to the ubiquitin/E1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8513-8518(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEXES WITH ZINC WITH OR
RP WITOUT ATP, COFACTOR, SUBUNIT, AND MUTAGENESIS OF TRP-174.
RX PubMed=15896804; DOI=10.1016/j.jmb.2005.04.011;
RA Duda D.M., Walden H., Sfondouris J., Schulman B.A.;
RT "Structural analysis of Escherichia coli ThiF.";
RL J. Mol. Biol. 349:774-786(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH ZINC AND SULFUR
RP CARRIER PROTEIN THIS, COFACTOR, AND REACTION MECHANISM.
RX PubMed=16388576; DOI=10.1021/bi051502y;
RA Lehmann C., Begley T.P., Ealick S.E.;
RT "Structure of the Escherichia coli ThiS-ThiF complex, a key component of
RT the sulfur transfer system in thiamin biosynthesis.";
RL Biochemistry 45:11-19(2006).
CC -!- FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the
CC C-terminal glycine of sulfur carrier protein ThiS.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly + ATP + H(+)
CC = [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + diphosphate;
CC Xref=Rhea:RHEA:43344, Rhea:RHEA-COMP:12909, Rhea:RHEA-COMP:12910,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.73;
CC Evidence={ECO:0000269|PubMed:9632726};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15896804, ECO:0000269|PubMed:16388576};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15896804,
CC ECO:0000269|PubMed:16388576};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15896804,
CC ECO:0000269|PubMed:16388576}.
CC -!- MASS SPECTROMETRY: Mass=26970.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10082377};
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M88701; AAB95618.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43090.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76966.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77327.1; -; Genomic_DNA.
DR PIR; C65206; C65206.
DR RefSeq; NP_418420.4; NC_000913.3.
DR RefSeq; WP_000999737.1; NZ_STEB01000045.1.
DR PDB; 1ZFN; X-ray; 2.75 A; A/B/C/D=1-251.
DR PDB; 1ZKM; X-ray; 2.95 A; A/B/C/D=1-251.
DR PDB; 1ZUD; X-ray; 1.98 A; 1/3=1-251.
DR PDBsum; 1ZFN; -.
DR PDBsum; 1ZKM; -.
DR PDBsum; 1ZUD; -.
DR AlphaFoldDB; P30138; -.
DR SMR; P30138; -.
DR BioGRID; 4262657; 10.
DR BioGRID; 852794; 2.
DR ComplexPortal; CPX-2134; ThiF-ThiS complex.
DR IntAct; P30138; 8.
DR STRING; 511145.b3992; -.
DR PaxDb; P30138; -.
DR PRIDE; P30138; -.
DR EnsemblBacteria; AAC76966; AAC76966; b3992.
DR EnsemblBacteria; BAE77327; BAE77327; BAE77327.
DR GeneID; 66672096; -.
DR GeneID; 948500; -.
DR KEGG; ecj:JW3956; -.
DR KEGG; eco:b3992; -.
DR PATRIC; fig|1411691.4.peg.2719; -.
DR EchoBASE; EB1546; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_3_6; -.
DR InParanoid; P30138; -.
DR OMA; SAKWKLE; -.
DR PhylomeDB; P30138; -.
DR BioCyc; EcoCyc:THIF-MON; -.
DR BioCyc; MetaCyc:THIF-MON; -.
DR BRENDA; 2.7.7.73; 2026.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; P30138; -.
DR PRO; PR:P30138; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902503; C:adenylyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990228; C:sulfurtransferase complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0018117; P:protein adenylylation; IDA:ComplexPortal.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0052837; P:thiazole biosynthetic process; IMP:EcoCyc.
DR InterPro; IPR012731; Adenyl_ThiF.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR02356; adenyl_thiF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Thiamine biosynthesis;
KW Thioester bond; Transferase; Zinc.
FT CHAIN 1..251
FT /note="Sulfur carrier protein ThiS adenylyltransferase"
FT /id="PRO_0000120578"
FT ACT_SITE 184
FT /note="Glycyl persulfide ester intermediate"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 127..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16388576"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16388576"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16388576"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:16388576"
FT CROSSLNK 184
FT /note="Glycyl cysteine dithioester (Cys-Gly) (interchain
FT with G-Cter in ThiS)"
FT MUTAGEN 174
FT /note="W->A: No adenylation of ThiS."
FT /evidence="ECO:0000269|PubMed:15896804"
FT MUTAGEN 184
FT /note="C->S: No cross-link formed with ThiS. No effect on
FT ThiS thiocarboxylate formation in vitro. Does not support
FT growth."
FT /evidence="ECO:0000269|PubMed:11438688"
FT CONFLICT 229..230
FT /note="WR -> C (in Ref. 1; AAB95618)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1ZUD"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1ZUD"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1ZFN"
FT HELIX 191..210
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1ZUD"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1ZUD"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1ZUD"
SQ SEQUENCE 251 AA; 26970 MW; 9CB9E20FD094F12D CRC64;
MNDRDFMRYS RQILLDDIAL DGQQKLLDSQ VLIIGLGGLG TPAALYLAGA GVGTLVLADD
DDVHLSNLQR QILFTTEDID RPKSQVSQQR LTQLNPDIQL TALQQRLTGE ALKDAVARAD
VVLDCTDNMA TRQEINAACV ALNTPLITAS AVGFGGQLMV LTPPWEQGCY RCLWPDNQEP
ERNCRTAGVV GPVVGVMGTL QALEAIKLLS GIETPAGELR LFDGKSSQWR SLALRRASGC
PVCGGSNADP V
