ID THII_METTH Reviewed; 389 AA.
AC O27720;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 01-MAY-2013, entry version 85.
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=MTH_1685;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
OS JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum
RT deltaH: functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA
CC to produce 4-thiouridine in position 8 of tRNAs, which functions
CC as a near-UV photosensor. Also catalyzes the transfer of sulfur to
CC the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate.
CC This is a step in the synthesis of thiazole, in the thiamine
CC biosynthesis pathway. The sulfur is donated as persulfide by IscS
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine +
CC tRNA containing a thionucleotide.
CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH +
CC [ThiS]-COSH + AMP.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the ThiI family.
CC -!- SIMILARITY: Contains 1 THUMP domain.
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DR EMBL; AE000666; AAB86157.1; -; Genomic_DNA.
DR PIR; C69092; C69092.
DR RefSeq; NP_276796.1; NC_000916.1.
DR ProteinModelPortal; O27720; -.
DR STRING; 187420.MTH1685; -.
DR EnsemblBacteria; AAB86157; AAB86157; MTH_1685.
DR GeneID; 1470770; -.
DR KEGG; mth:MTH1685; -.
DR eggNOG; COG0301; -.
DR KO; K03151; -.
DR OMA; FGIQAFS; -.
DR ProtClustDB; CLSK2392172; -.
DR BioCyc; MTHE187420:GJNM-1687-MONOMER; -.
DR UniPathway; UPA00060; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:HAMAP.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00021; ThiI; 1; -.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR003720; ThiI.
DR InterPro; IPR020536; ThiI_C_dom.
DR InterPro; IPR004114; THUMP.
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 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding;
KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase;
KW tRNA-binding.
FT CHAIN 1 389 Probable tRNA sulfurtransferase.
FT /FTId=PRO_0000154896.
FT DOMAIN 57 165 THUMP.
FT NP_BIND 183 184 ATP (By similarity).
FT BINDING 267 267 ATP (By similarity).
FT BINDING 289 289 ATP; via amide nitrogen (By similarity).
FT BINDING 298 298 ATP (By similarity).
SQ SEQUENCE 389 AA; 42473 MW; CBB6B788018AACE6 CRC64;
MILDYDVILA RYGEVAIKGP SVRRRFEGKL LHNIKSAFSC RAELRHGRIF IFPEDMDEAL
DRLSKIFGIV SFSPAVTAET GFDSIEDSLR EYIHELRSEG LLTSRTPFAI RCRRVGEHDF
TSQEMAAFAG SVVVGEIGAP VDLGNPDLEI HLEIREDETY IYHRVIPGPG GLPAGTQGKV
VALLSGGIDS PVATYLMMKR GCQVVAVHMD NAPFTGEEAE EKVEKIAAKL AEYSAGVEFK
LRTFSYGRYL ESCRRGAPEK MTCVLCKFGM YHLAEMVAEE EGALAIVDGS SLGQVASQTL
PNILATRMGV NIPILSPLIG MDKVEIENLA KRIGTYDISV IPDGGCSAVP AHPSTASPPE
AVMEASEKIN VKEEVAEIFR KGSKTRIFS
//
