Q2RM06 (THII_MOOTA) 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:	Moth_0198

Organism

Moorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]

Taxonomic identifier

264732 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella › Moorella thermoacetica

Protein attributes

Sequence length	390 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.
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 – 390	390	Probable tRNA sulfurtransferase HAMAP-Rule MF_00021		PRO_1000074245
Regions
	Domain	58 – 161	104	THUMP
	Nucleotide binding	179 – 180	2	ATP By similarity
	Nucleotide binding	204 – 205	2	ATP By similarity
Sites
	Binding site	261	1	ATP By similarity
	Binding site	283	1	ATP; via amide nitrogen By similarity
	Binding site	292	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2RM06 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 035FB245B58B5538	FASTA	390	43,237
	10 20 30 40 50 60 MYTSLLVRYG EISLKGNNRP YFEDKLLANM RRALAGLPPR RMRKTFGRVF VELHDDLEAV 70 80 90 100 110 120 ARRLQRVFGI VSMSPVATAP LELEAIKKAA LAVLKDSPGS TFKVQAQRPN KRFPLTSPEV 130 140 150 160 170 180 NQELGAYLLT HSQGQRVDVH HPDRVIHVEI RDEGAYIYSR IIPGPGGLPV GVTGRGLLLI 190 200 210 220 230 240 SGGIDSPVAG YMGMKRGLEL TALHFHSFPF TSERSKEKVI DLCRVLAGYS GPLRLVVAPF 250 260 270 280 290 300 TNIQKAIRQN CPQEFYVTIM RRMMFRIARA VAAKEEAPAI LTGESLGQVA SQTLQSMAVI 310 320 330 340 350 360 NKVVDLPVLR PLVAWDKSEI IEVARRIGTY DISIRPYEDC CTLFVPKHPA TKPPLARVEA 370 380 390 AEKNLAVVEL VAECLENLEI LTVEPEADVV

References

[1]

"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)." Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W. Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39073.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000232 Genomic DNA. Translation: ABC18533.1.
RefSeq	YP_429076.1. NC_007644.1.
3D structure databases
HSSP	HSSP built from PDB template 2C5S based on UniProtKB Q81KU0.
ProteinModelPortal	Q2RM06.
ModBase	Search...
Protein-protein interaction databases
STRING	264732.Moth_0198.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABC18533; ABC18533; Moth_0198.
GeneID	3832271.
KEGG	mta:Moth_0198.
PATRIC	22637419. VBIMooThe6753_0210.
Phylogenomic databases
eggNOG	COG0301.
HOGENOM	HOG000227470.
KO	K03151.
OMA	FGIQAFS.
ProtClustDB	PRK01565.
Enzyme and pathway databases
BioCyc	MTHE264732:GH0A-290-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_MOOTA

Accession

Primary (citable) accession number: Q2RM06

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program