SPM_000915


  Uniprot: A0A037UQ10
Description: thiamine biosynthesis protein ThiI
EC number: 2.8.1.4
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498918}.; CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498909}.
Cofactor: 
Enzyme regulation: 
Function [CC]: 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. {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498907}.
Pathway: PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498911}.
Active site: 
Binding site: BINDING 266 266 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.; BINDING 288 288 ATP; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_00021}.; BINDING 297 297 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: NP_BIND 182 183 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.; NP_BIND 207 208 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
Site: 
Gene names (primary): thiI
Gene names (synonym): 
Mass: 45,467
Subunit structure [CC]: 
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; sulfurtransferase activity [GO:0016783]; tRNA adenylyltransferase activity [GO:0004810]; tRNA binding [GO:0000049]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]; tRNA thio-modification [GO:0034227]
Gene ontology IDs: GO:0000049; GO:0004810; GO:0005524; GO:0005737; GO:0009228; GO:0009229; GO:0016783; GO:0034227
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00543539}.; SIMILARITY: Contains 1 THUMP domain. {ECO:0000256|HAMAP-Rule:MF_00021}.
Protein families: ThiI family
Coiled coil: 
Domain [FT]: DOMAIN 62 164 THUMP. {ECO:0000259|PROSITE:PS51165}.
Motif: 
Region: 
EMBL: AGBZ02000001
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92646
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 3.40.50.620
InterPro: MF_00021
PANTHER: IPR014729;IPR020536;IPR004114;IPR003720
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: PS51165
ProDom: PF02568;PF02926
SMART: 
SUPFAM: SM00981
TIGRFAMs: 
173185-174385(-)

>nucleotide sequence
CTAGTTTTCTTCTTCATAAATCACATCCTTACCAACGACATATGTTTTTATATTTTTTTT
AATTATAACATCAATAATTTCTGCTCACATTAAATTTTTTTCTTGAAATTCTGCTTGTTT
TATCCGTGGTTTTGTAACCGGATTCTTTGGAACAAATAAACTACAACAATCTTCAAATGG
TAAAATTGATGTCTGATAAGTATCAATTTGTTTTGCAATATCAATGATTTCATTTTTATC
AAAACATAATACTGGTCGCAAAATTGGCAATGTAGAAACAGCATTGATCGTATTAATACT
TTCAATTGTTTGCGAAGCAACTTGCCCCAATGATTCTCCAGTAATAATTGCCTGACATTT
TAATTCTTTGGCTAATAAATTAGCGATCCGATAAAACATTCGTCGCATAATAATAATTCG
ATAACTAGCATCAGGAATATGCATTAATTCATGTTGTAACATTGAAAAATTAACCACATG
CAAGCGCTGCTGATTTTGACCAGCATAATAATTTAATTTTTGAACTAAAGTTTTAACCTT
TTGTAATGCTTCTTCAGTCGTATGTGGTGGTGTTGCAAAATGTAAATATTCAACATTCAT
GCCCCGTTTCATTGTTAAAAAAGACGCAACTGGTGAATCAATTCCCCCCGATAGCATTAC
TAATCCTTGACCAGATATTCCAACTGGTAAACCACCAATTGTTTTAATTTTATTAACAAA
AACATATGTAAATGTTCGTCGTACTTCAACATCAATTTGTAAAACTGGTTGATGAACATC
AACCTTAACCTTTGTTTGTTGTAATATTTTTGGTGCTAATTGTTGTTTAATTTCTGTCGA
TGTAAGTGGAAAAGTCTTATCATTTCGGCGCACTTCTAATTTAAAAGTTGCTGGTTGATA
ATAATTTACAATATTAATTGCACAATTAGCAATTTCTGATAAATCACAACTAACCTTTTT
GGCTAATGATAAAGATGATGAACCAAAAACATTTTTAACAATGTTAACAATTTCTATACT
AACTGTTGCATCTAATAATTCAATAAATAAACGATCAAATTCTTTTTTAAGTTGATATTG
ATTTTCATAGGCTACTAATTTTGTTTTAATATTATTAACTAAAACTCTTGTAAAATTATT
ACGGTTTTTCCCTTTTGTTGTTAATTCCCCATAACGAATTAATATTACATCAAAATTCAT


>protein sequence
MNFDVILIRYGELTTKGKNRNNFTRVLVNNIKTKLVAYENQYQLKKEFDRLFIELLDATV
SIEIVNIVKNVFGSSSLSLAKKVSCDLSEIANCAINIVNYYQPATFKLEVRRNDKTFPLT
STEIKQQLAPKILQQTKVKVDVHQPVLQIDVEVRRTFTYVFVNKIKTIGGLPVGISGQGL
VMLSGGIDSPVASFLTMKRGMNVEYLHFATPPHTTEEALQKVKTLVQKLNYYAGQNQQRL
HVVNFSMLQHELMHIPDASYRIIIMRRMFYRIANLLAKELKCQAIITGESLGQVASQTIE
SINTINAVSTLPILRPVLCFDKNEIIDIAKQIDTYQTSILPFEDCCSLFVPKNPVTKPRI
KQAEFQEKNLMWAEIIDVIIKKNIKTYVVGKDVIYEEEN






















© Fisunov Lab of Proteomics, 2016.