THII_BACAN
ID THII_BACAN Reviewed; 403 AA.
AC Q81KU0; Q6HS96; Q6KLJ3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable tRNA sulfurtransferase;
DE EC=2.8.1.4;
DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase;
DE AltName: Full=Thiamine biosynthesis protein ThiI;
DE AltName: Full=tRNA 4-thiouridine synthase;
GN Name=thiI; OrderedLocusNames=BA_4899, GBAA_4899, BAS4545;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMP.
RX PubMed=16343540; DOI=10.1016/j.jmb.2005.11.013;
RA Waterman D.G., Ortiz-Lombardia M., Fogg M.J., Koonin E.V., Antson A.A.;
RT "Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme
RT containing the predicted RNA-binding THUMP domain.";
RL J. Mol. Biol. 356:97-110(2006).
CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to
CC produce 4-thiouridine in position 8 of tRNAs, which functions as a
CC near-UV photosensor. Also catalyzes the transfer of sulfur to the
CC sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a
CC step in the synthesis of thiazole, in the thiamine biosynthesis
CC pathway. The sulfur is donated as persulfide by IscS (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a
CC uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] =
CC [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA +
CC AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338, Rhea:RHEA-COMP:13339,
CC Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:61963, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:136798, ChEBI:CHEBI:456215; EC=2.8.1.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + AH2 +
CC S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-carrier
CC protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-
CC cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340, Rhea:RHEA-
CC COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12908, Rhea:RHEA-
CC COMP:12910, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90619, ChEBI:CHEBI:456215;
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT56842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP28584.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34017.2; -; Genomic_DNA.
DR EMBL; AE017225; AAT56842.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_847098.1; NC_003997.3.
DR RefSeq; YP_030792.1; NC_005945.1.
DR PDB; 2C5S; X-ray; 2.50 A; A=1-403.
DR PDBsum; 2C5S; -.
DR AlphaFoldDB; Q81KU0; -.
DR SMR; Q81KU0; -.
DR STRING; 260799.BAS4545; -.
DR DNASU; 1087273; -.
DR EnsemblBacteria; AAP28584; AAP28584; BA_4899.
DR EnsemblBacteria; AAT34017; AAT34017; GBAA_4899.
DR KEGG; ban:BA_4899; -.
DR KEGG; bar:GBAA_4899; -.
DR KEGG; bat:BAS4545; -.
DR PATRIC; fig|198094.11.peg.4859; -.
DR eggNOG; COG0301; Bacteria.
DR HOGENOM; CLU_037952_4_0_9; -.
DR OMA; SMPEFCG; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; Q81KU0; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140741; F:tRNA U4 sulfurtransferase; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR CDD; cd01712; ThiI; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00021; ThiI; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020536; ThiI_AANH.
DR InterPro; IPR004114; THUMP_dom.
DR InterPro; IPR003720; tRNA_STrfase.
DR Pfam; PF02568; ThiI; 1.
DR Pfam; PF02926; THUMP; 1.
DR SMART; SM00981; THUMP; 1.
DR TIGRFAMs; TIGR00342; TIGR00342; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase;
KW tRNA-binding.
FT CHAIN 1..403
FT /note="Probable tRNA sulfurtransferase"
FT /id="PRO_0000154830"
FT DOMAIN 60..165
FT /note="THUMP"
FT BINDING 183..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 208..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:2C5S"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 72..84
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 156..167
FT /evidence="ECO:0007829|PDB:2C5S"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:2C5S"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 260..278
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2C5S"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:2C5S"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:2C5S"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2C5S"
SQ SEQUENCE 403 AA; 45711 MW; A87E445661268FA6 CRC64;
MTYEYILVRY GEMTTKGKNR SKFVSTLKDN VKFKLKKFPN IKIDATHDRM YIQLNGEDHE
AVSERLKDVF GIHKFNLAMK VPSELEDIKK GALAAFLQVK GDVKTFKITV HRSYKHFPMR
TMELLPEIGG HILENTEDIT VDVHNPDVNV RVEIRSGYSY IMCDERMGAG GLPVGVGGKV
MVLLSGGIDS PVAAYLTMKR GVSVEAVHFH SPPFTSERAK QKVIDLAQEL TKYCKRVTLH
LVPFTEVQKT INKEIPSSYS MTVMRRMMMR ITERIAEERN ALAITTGESL GQVASQTLDS
MHTINEVTNY PVIRPLITMD KLEIIKIAEE IGTYDISIRP YEDCCTVFTP ASPATKPKRE
KANRFEAKYD FTPLIDEAVA NKETMVLQTV EVVAEEEKFE ELF
