SUA5_BACSU
ID SUA5_BACSU Reviewed; 346 AA.
AC P39153;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 YwlC;
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein YwlC;
GN Name=ywlC; OrderedLocusNames=BSU36950; ORFNames=ipc-29d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Glaser P., Danchin A.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP COMPLEMENTATION OF YEAST MUTANTS.
RC STRAIN=168;
RX PubMed=19287007; DOI=10.1093/nar/gkp152;
RA El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F.,
RA Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V.;
RT "The universal YrdC/Sua5 family is required for the formation of
RT threonylcarbamoyladenosine in tRNA.";
RL Nucleic Acids Res. 37:2894-2909(2009).
RN [4]
RP FUNCTION AS A TC-AMP SYNTHASE, AND CATALYTIC ACTIVITY.
RC STRAIN=168;
RX PubMed=23072323; DOI=10.1021/bi301233d;
RA Lauhon C.T.;
RT "Mechanism of N6-threonylcarbamoyladenosine (t(6)A) biosynthesis: isolation
RT and characterization of the intermediate threonylcarbamoyl-AMP.";
RL Biochemistry 51:8950-8963(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. 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. Is also able to catalyze
CC the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP
CC and PPi. {ECO:0000269|PubMed:23072323}.
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:0000269|PubMed:23072323};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Complements a S.cerevisiae SUA5 disruption mutant.
CC -!- MISCELLANEOUS: The four proteins YwlC, TsaD, TsaB and TsaE are
CC necessary and sufficient for tRNA(NNU) t(6)A37
CC threonylcarbamoyladenosine biosynthesis in vitro in B.subtilis.
CC {ECO:0000305|PubMed:23072323}.
CC -!- MISCELLANEOUS: Unlike previously thought, the formation of TC-AMP does
CC not proceed via an ATP-activated HCO(3)(-) intermediate such as
CC carboxy-AMP. {ECO:0000305|PubMed:23072323}.
CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
CC -!- CAUTION: The well-known t(6)A modification appears to be a hydrolyzed
CC artifact of natural cyclic t(6)A (ct(6)A) that occurs during the
CC preparation and handling of tRNA in B.subtilis and many other species
CC (PubMed:23242255). In these species, the t(6)A modification is
CC processed further by dehydration into ct(6)A, a reaction catalyzed by
CC TcdA. {ECO:0000305}.
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DR EMBL; Z38002; CAA86105.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15712.1; -; Genomic_DNA.
DR PIR; I40476; I40476.
DR RefSeq; NP_391576.1; NC_000964.3.
DR RefSeq; WP_003227659.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39153; -.
DR SMR; P39153; -.
DR STRING; 224308.BSU36950; -.
DR PaxDb; P39153; -.
DR PRIDE; P39153; -.
DR EnsemblBacteria; CAB15712; CAB15712; BSU_36950.
DR GeneID; 937023; -.
DR KEGG; bsu:BSU36950; -.
DR PATRIC; fig|224308.179.peg.4002; -.
DR eggNOG; COG0009; Bacteria.
DR InParanoid; P39153; -.
DR OMA; GMLKSHY; -.
DR PhylomeDB; P39153; -.
DR BioCyc; BSUB:BSU36950-MON; -.
DR BRENDA; 2.7.7.87; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
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 ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..346
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000202020"
FT DOMAIN 18..205
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT BINDING 40
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37007 MW; 06E16DD5D4586E7B CRC64;
MKTKRWFVDV TDELSTNDPQ IAQAAALLRE NEVVAFPTET VYGLGANAKN TDAVKKIYEA
KGRPSDNPLI VHIADISQLE DLTGPAPEKA KTLMKRFWPG ALTLILPCKP DALSPRVTAG
LETVAIRMPD HPLALALIRE SGLPIAAPSA NLSGKPSPTK AEHVAHDLDG RIAGIVDGGP
TGIGVESTVL SCADDIPVLL RPGGITKEQI EAVIGPIHVD KGLSDQNEKP ISPGMKYTHY
APTAPLAICE GSPERIQHLI QEYQQGGRRV GVLTTEEKAG VYSADYVKSC GRRAQLETVA
AGLYDALRSF DENKVDFIIA ESFPDTGVGL AIMNRLMKAA GGRVIR
