SUA5_SULTO
ID SUA5_SULTO Reviewed; 352 AA.
AC Q970S6;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Threonylcarbamoyl-AMP synthase;
DE Short=TC-AMP synthase;
DE EC=2.7.7.87;
DE AltName: Full=L-threonylcarbamoyladenylate synthase;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Sua5;
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Sua5;
GN Name=sua5; OrderedLocusNames=STK_15260;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX
RP WITH AMP, ATPASE ACTIVITY, AND SUBUNIT.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=18004774; DOI=10.1002/prot.21794;
RA Agari Y., Sato S., Wakamatsu T., Bessho Y., Ebihara A., Yokoyama S.,
RA Kuramitsu S., Shinkai A.;
RT "X-ray crystal structure of a hypothetical Sua5 protein from Sulfolobus
RT tokodaii strain 7.";
RL Proteins 70:1108-1111(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH L-THREONINE AND AN
RP ATP ANALOG, THREONINE-BINDING, ATP-BINDING, AND SUBUNIT.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=21538543; DOI=10.1002/prot.23026;
RA Kuratani M., Kasai T., Akasaka R., Higashijima K., Terada T., Kigawa T.,
RA Shinkai A., Bessho Y., Yokoyama S.;
RT "Crystal structure of Sulfolobus tokodaii Sua5 complexed with L-threonine
RT and AMPPNP.";
RL Proteins 79:2065-2075(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP THREONYLCARBAMOYLADENYLATE, AND FUNCTION.
RX PubMed=22383337; DOI=10.1002/anie.201108896;
RA Parthier C., Gorlich S., Jaenecke F., Breithaupt C., Brauer U.,
RA Fandrich U., Clausnitzer D., Wehmeier U.F., Bottcher C., Scheel D.,
RA Stubbs M.T.;
RT "The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction.";
RL Angew. Chem. Int. Ed. 51:4046-4052(2012).
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 (By similarity). Probably catalyzes the conversion of L-
CC threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-
CC AMP) as the acyladenylate intermediate, with the release of
CC diphosphate. Shows ATP hydrolysis activity in vitro, producing AMP.
CC {ECO:0000250, ECO:0000269|PubMed:22383337}.
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18004774,
CC ECO:0000269|PubMed:21538543, ECO:0000269|PubMed:22383337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR EMBL; BA000023; BAB66597.1; -; Genomic_DNA.
DR RefSeq; WP_010979575.1; NC_003106.2.
DR PDB; 2EQA; X-ray; 1.80 A; A=1-352.
DR PDB; 3AJE; X-ray; 1.80 A; A=1-352.
DR PDB; 4E1B; X-ray; 1.80 A; A=1-352.
DR PDBsum; 2EQA; -.
DR PDBsum; 3AJE; -.
DR PDBsum; 4E1B; -.
DR AlphaFoldDB; Q970S6; -.
DR SMR; Q970S6; -.
DR STRING; 273063.STK_15260; -.
DR EnsemblBacteria; BAB66597; BAB66597; STK_15260.
DR GeneID; 1459561; -.
DR KEGG; sto:STK_15260; -.
DR PATRIC; fig|273063.9.peg.1733; -.
DR eggNOG; arCOG01952; Archaea.
DR OMA; GMLKSHY; -.
DR OrthoDB; 52427at2157; -.
DR BRENDA; 2.7.7.87; 15396.
DR EvolutionaryTrace; Q970S6; -.
DR PRO; PR:Q970S6; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11030; -; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR038385; Sua5/YwlC_C.
DR InterPro; IPR005145; Sua5_C.
DR InterPro; IPR010923; T(6)A37_SUA5.
DR InterPro; IPR006070; YrdC-like_dom.
DR Pfam; PF03481; SUA5; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR PIRSF; PIRSF004930; Tln_factor_SUA5; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00057; TIGR00057; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18004774"
FT CHAIN 2..352
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000423850"
FT DOMAIN 14..200
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT BINDING 36
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:21538543"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 68
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:21538543"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 122
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:21538543"
FT BINDING 142
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:21538543"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 182
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:21538543"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:2EQA"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3AJE"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:2EQA"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 291..307
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2EQA"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3AJE"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:2EQA"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2EQA"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:2EQA"
SQ SEQUENCE 352 AA; 38802 MW; A1D5B9FA171BD294 CRC64;
MTQIIKIDPL NPEIDKIKIA ADVIRNGGTV AFPTETVYGL GANAFDGNAC LKIFQAKNRP
VDNPLIVHIA DFNQLFEVAK DIPDKVLEIA QIVWPGPLTF VLKKTERVPK EVTAGLDTVA
VRMPAHPIAL QLIRESGVPI AAPSANLATR PSPTKAEDVI VDLNGRVDVI IDGGHTFFGV
ESTIINVTVE PPVLLRPGPF TIEELKKLFG EIVIPEFAQG KKEAEIALAP GMKYKHYAPN
TRLLLVENRN IFKDVVSLLS KKYKVALLIP KELSKEFEGL QQIILGSDEN LYEVARNLFD
SFRELDKLNV DLGIMIGFPE RGIGFAIMNR ARKASGFSII KAISDVYKYV NI
