位置:首页 > 蛋白库 > TSAC_SHEWM
TSAC_SHEWM
ID   TSAC_SHEWM              Reviewed;         185 AA.
AC   B1KCX0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
GN   Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN;
GN   OrderedLocusNames=Swoo_0044;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2)
CC       and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate
CC       intermediate, with the release of diphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01852}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01852};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
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; CP000961; ACA84345.1; -; Genomic_DNA.
DR   RefSeq; WP_012322694.1; NC_010506.1.
DR   AlphaFoldDB; B1KCX0; -.
DR   SMR; B1KCX0; -.
DR   STRING; 392500.Swoo_0044; -.
DR   EnsemblBacteria; ACA84345; ACA84345; Swoo_0044.
DR   KEGG; swd:Swoo_0044; -.
DR   eggNOG; COG0009; Bacteria.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   OMA; LVDAFWP; -.
DR   OrthoDB; 1913202at2; -.
DR   Proteomes; UP000002168; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01852; TsaC; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR023535; TC-AMP_synthase.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   PANTHER; PTHR17490:SF8; PTHR17490:SF8; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00057; TIGR00057; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..185
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000352990"
FT   DOMAIN          3..185
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ   SEQUENCE   185 AA;  20101 MW;  C246267C3A30CC37 CRC64;
     MLEQAPAEVK QVIESGGVVA YPTEAVYGLG CDPDNDAAIT KLLAIKKRPW EKGLILVASD
     YQQLLPYIDD SQLTEEQRER VFSKWPGPFT FIMPIKPGIS NLLCGSFNSL AVRVSDHPTI
     QAICQQLGKP LVSTSANHSG EEPAMSHEEI LAKFEGEIDA LVAGSLGEQR KPSTIIDAIS
     GKILR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024