(data stored in ACNUC10043 zone)

SWISSPROT: E1RKE1_METP4

ID   E1RKE1_METP4            Unreviewed;       391 AA.
AC   E1RKE1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   11-DEC-2019, entry version 58.
DE   RecName: Full=Probable tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021};
DE            EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000256|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000256|HAMAP-Rule:MF_00021};
GN   OrderedLocusNames=Mpet_1027 {ECO:0000313|EMBL:ADN35794.1};
OS   Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS   (Methanoplanus petrolearius).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX   NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN35794.1, ECO:0000313|Proteomes:UP000006565};
RN   [1] {ECO:0000313|EMBL:ADN35794.1, ECO:0000313|Proteomes:UP000006565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC   {ECO:0000313|Proteomes:UP000006565};
RX   PubMed=21304750;
RA   Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA   Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT   4847).";
RL   Stand. Genomic Sci. 3:203-211(2010).
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00021}.
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         Evidence={ECO:0000256|HAMAP-Rule:MF_00021};
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00021};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00021}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002117; ADN35794.1; -; Genomic_DNA.
DR   STRING; 679926.Mpet_1027; -.
DR   EnsemblBacteria; ADN35794; ADN35794; Mpet_1027.
DR   KEGG; mpi:Mpet_1027; -.
DR   eggNOG; arCOG00038; Archaea.
DR   eggNOG; COG0301; LUCA.
DR   HOGENOM; HOG000227470; -.
DR   KO; K03151; -.
DR   OMA; SMPEFCG; -.
DR   OrthoDB; 57901at2157; -.
DR   BioCyc; MPET679926:G1GN5-1054-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000006565; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; 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: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   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   3: Inferred from homology;
DR   PRODOM; E1RKE1.
DR   SWISS-2DPAGE; E1RKE1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00021};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006565};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE-
KW   ProRule:PRU00529}; Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00021};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   DOMAIN          54..158
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
FT   NP_BIND         176..177
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   NP_BIND         201..202
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         263
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         285
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         294
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   391 AA;  42497 MW;  E0C64B8AB34C2399 CRC64;
     MIRYGELFLK SEPVMRHYVG VLTANIKRAL DAEEICHEIT ITRGRIFVYG EDVDAINSVL
     LRIFGIVGTS IVICTPPDRE TIEKTAAIVA SRTLKPGMSF AVRARRSNIK GFTSQELAAS
     TGSCIYEAVG DLKVDLDNPE YEIFIEARSN GGFIYETRTP GPGGLPVGTQ GKVLCLLSAG
     IDSPVAAWLA MSRGCIPGFI YFDGGDYFGK DTNRAVLENL QNLSRWYPGS TVEAAFIDIT
     PFFDKLTDKS AKEALKNRCI ICKRFMLRLA GKCALDWKYL GLVTGNSIGQ VASQTLANIG
     ILGSAVPEGI ALIEPLITYD KEDTVKIARN IGTFRENAGD LSCGVVPSHP SIAATLAKVI
     EDEGMLGIPE LIEECIPRKT IYKAKDGKLL D
//

If you have problems or comments...

PBIL Back to PBIL home page