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THII_GEOTN
ID   THII_GEOTN              Reviewed;         401 AA.
AC   A4IRT9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE            EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021}; OrderedLocusNames=GTNG_2698;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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:0000255|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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00021};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00021}.
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DR   EMBL; CP000557; ABO68043.1; -; Genomic_DNA.
DR   RefSeq; WP_011887981.1; NC_009328.1.
DR   AlphaFoldDB; A4IRT9; -.
DR   SMR; A4IRT9; -.
DR   STRING; 420246.GTNG_2698; -.
DR   EnsemblBacteria; ABO68043; ABO68043; GTNG_2698.
DR   KEGG; gtn:GTNG_2698; -.
DR   eggNOG; COG0301; Bacteria.
DR   HOGENOM; CLU_037952_4_0_9; -.
DR   OMA; SMPEFCG; -.
DR   OrthoDB; 773697at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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:0140741; F:tRNA U4 sulfurtransferase; IEA:UniProtKB-EC.
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   CDD; cd01712; ThiI; 1.
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;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; RNA-binding;
KW   Thiamine biosynthesis; Transferase; tRNA-binding.
FT   CHAIN           1..401
FT                   /note="Probable tRNA sulfurtransferase"
FT                   /id="PRO_1000074226"
FT   DOMAIN          60..165
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         183..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         208..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   401 AA;  45401 MW;  54C12B5796DF8721 CRC64;
     MKYDRILIRY GEMTTKGKNR NIFVRRLKNN IARKLQAFPR IKIEYMRDRM YILLNGEPHE
     PIIDKLKTVF GIHSFSLAMK CENDLAAIKE TALAAVRQLP YKGKTFKVSA RRVDKQFPYR
     SDELNHEVGA HILRQTEDLT VNVRQPDIDV RIEVRQDGTY VTCHDIFGAG GLPVGTSGKA
     MLMLSGGIDS PVAGYLAMKR GLEIEAVHFF SPPFTSERAK QKVIDLVRKL TAYGGKIKLH
     IVPFTEVQQA IYQGVPNEYS LISTRRAMLK ITDALRRRQR GLAIVTGESL GQVASQTLES
     MYVINEVTNT PVLRPLISMD KMEIIEIAKQ IDTHDISILP YEDCCTIFTP RAPKTKPKKE
     KVLQHESQLD LAPLLEKAIN ETETIVIDEE AGQADEFTAL F
 
 
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