SUA5_PYRAB
ID SUA5_PYRAB Reviewed; 340 AA.
AC Q9UYB2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PYRAB15960; ORFNames=PAB1302;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION IN T(6)A TRNA MODIFICATION, AND LACK OF TRNA-BINDING.
RC STRAIN=GE5 / Orsay;
RX PubMed=23258706; DOI=10.1093/nar/gks1287;
RA Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B.,
RA van Tilbeurgh H., Forterre P., Basta T.;
RT "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and
RT Eukarya.";
RL Nucleic Acids Res. 41:1953-1964(2013).
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. Likely catalyzes the conversion of L-threonine,
CC HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the
CC acyladenylate intermediate, with the release of diphosphate. Does not
CC bind tRNA. {ECO:0000269|PubMed:23258706}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR EMBL; AJ248288; CAB50500.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71055.1; -; Genomic_DNA.
DR PIR; F75007; F75007.
DR RefSeq; WP_010868714.1; NC_000868.1.
DR PDB; 6F87; X-ray; 2.62 A; A/B/C/D=2-340.
DR PDB; 6F89; X-ray; 2.81 A; A/B=1-340.
DR PDB; 6F8Y; X-ray; 2.86 A; A/B/C/D=2-340.
DR PDBsum; 6F87; -.
DR PDBsum; 6F89; -.
DR PDBsum; 6F8Y; -.
DR AlphaFoldDB; Q9UYB2; -.
DR SMR; Q9UYB2; -.
DR STRING; 272844.PAB1302; -.
DR PRIDE; Q9UYB2; -.
DR EnsemblBacteria; CAB50500; CAB50500; PAB1302.
DR GeneID; 1495884; -.
DR KEGG; pab:PAB1302; -.
DR PATRIC; fig|272844.11.peg.1702; -.
DR eggNOG; arCOG01952; Archaea.
DR HOGENOM; CLU_031397_0_0_2; -.
DR OMA; GMLKSHY; -.
DR OrthoDB; 52427at2157; -.
DR PhylomeDB; Q9UYB2; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase; tRNA processing.
FT CHAIN 1..340
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000423851"
FT DOMAIN 13..199
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT BINDING 35
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:6F87"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6F87"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:6F87"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:6F87"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6F87"
SQ SEQUENCE 340 AA; 37446 MW; CBEA8D74FE548B7F CRC64;
MTIIINVRER IEEWKIRIAA GFIREGKLVA FPTETVYGLG ANALDENAVK RIFEAKGRPA
DNPLIIHIAS FEQLEVLAKE IPEEAEMLAK RFWPGPLTLV LPKSEVVPRV ITGGLDTVAV
RMPAHEIALK LIELSERPIA APSANISGKP SPTSAHHVAE DFYGKIECII DGGETRIGVE
STVIDLTEWP PVLLRPGGLP LEEIEKVIGE IRIHPAVYGK SVDTAKAPGM KYRHYAPSAE
VIVVEGPRDK VRRKIEELIA KFKEEGKKVG VIGSGSYDAD EVFYLGDTVE EIARNLFKAL
RHMDRTGVDV ILAEGVEEKG LGLAVMNRLR KASGYRIIKV
