Q83CD9 (THII_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable tRNA sulfurtransferase
EC=2.8.1.4

Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferase
Thiamine biosynthesis protein ThiI
tRNA 4-thiouridine synthase

Gene names

Name:	thiI
Ordered Locus Names:	CBU_1181

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS By similarity. HAMAP-Rule MF_00021
Catalytic activity	L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. HAMAP-Rule MF_00021 [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. HAMAP-Rule MF_00021
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00021
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00021.
Sequence similarities	Belongs to the ThiI family. Contains 1 THUMP domain.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA thio-modification Inferred from electronic annotation. Source: HAMAP thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP sulfurtransferase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 392	392	Probable tRNA sulfurtransferase HAMAP-Rule MF_00021		PRO_0000154836
Regions
	Domain	59 – 166	108	THUMP
	Nucleotide binding	186 – 187	2	ATP By similarity
	Nucleotide binding	211 – 212	2	ATP By similarity
Sites
	Binding site	269	1	ATP By similarity
	Binding site	290	1	ATP; via amide nitrogen By similarity
	Binding site	299	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83CD9 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: ECE42AFA1F6E0AE7	FASTA	392	44,677
	10 20 30 40 50 60 MKKVILIKYG EIALKGKNRH LFESSIIENI RLAIGEGAPP IEQCRGRLYL QLTTEKDISC 70 80 90 100 110 120 YREALKRVFG VVGFALAYRL NLEINLEEME EVLIKHLRKL ESKSLAFRVD TRRTVKSFPM 130 140 150 160 170 180 DSMEINKKLG ALILQHFPKW QVNLNNPELT IFIEVRDEGL FIYTTEDHED GLGGLPVGVG 190 200 210 220 230 240 GRGLLLLSGG IDSPVAGWTL LKRGMMIDAV YFHSFPYTGE KAKEKVIDLA RVLTSWKLRA 250 260 270 280 290 300 INLHIPYFTK IQETVNKMCP ESTWTIIHRR FMMRIAEKLT KSTYHTLITG ENLGQVASQT 310 320 330 340 350 360 IQNIAVINQA TNLPILRPLI SFDKNDIIKI AEKIGTFRIS KRPYEDCCAL FAPKNPETKA 370 380 390 KEEAILKAEE NLPLNELINE ALEKMETLRI KN

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90690.1.
RefSeq	NP_820176.1. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83CD9.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_1181.
Proteomic databases
PRIDE	Q83CD9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90690; AAO90690; CBU_1181.
GeneID	1209084.
KEGG	cbu:CBU_1181.
PATRIC	17931103. VBICoxBur82552_1178.
Phylogenomic databases
eggNOG	COG0301.
HOGENOM	HOG000227470.
KO	K03151.
OMA	FGIQAFS.
ProtClustDB	PRK01565.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-1167-MONOMER.
UniPathway	UPA00060.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00021. ThiI.
InterPro	IPR014729. Rossmann-like_a/b/a_fold. IPR003720. ThiI. IPR020536. ThiI_C_dom. IPR004114. THUMP. [Graphical view]
Pfam	PF02568. ThiI. 1 hit. PF02926. THUMP. 1 hit. [Graphical view]
SMART	SM00981. THUMP. 1 hit. [Graphical view]
TIGRFAMs	TIGR00342. TIGR00342. 1 hit.
PROSITE	PS51165. THUMP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THII_COXBU

Accession

Primary (citable) accession number: Q83CD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program