(data stored in SCRATCH zone)

SWISSPROT: Q5LX83_RUEPO

ID   Q5LX83_RUEPO            Unreviewed;       316 AA.
AC   Q5LX83;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|PIRNR:PIRNR004930};
DE            Short=TC-AMP synthase {ECO:0000256|PIRNR:PIRNR004930};
DE            EC=2.7.7.87 {ECO:0000256|PIRNR:PIRNR004930};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|PIRNR:PIRNR004930};
GN   OrderedLocusNames=SPO0297 {ECO:0000313|EMBL:AAV93615.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93615.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93615.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93615.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine. {ECO:0000256|PIRNR:PIRNR004930}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O
CC         + L-threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:73682;
CC         EC=2.7.7.87; Evidence={ECO:0000256|PIRNR:PIRNR004930};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}.
CC   -!- SIMILARITY: Belongs to the SUA5 family.
CC       {ECO:0000256|PIRNR:PIRNR004930, ECO:0000256|SAAS:SAAS00696307}.
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DR   EMBL; CP000031; AAV93615.1; -; Genomic_DNA.
DR   RefSeq; WP_011046058.1; NC_003911.12.
DR   STRING; 246200.SPO0297; -.
DR   EnsemblBacteria; AAV93615; AAV93615; SPO0297.
DR   KEGG; sil:SPO0297; -.
DR   eggNOG; ENOG4107QIS; Bacteria.
DR   eggNOG; COG0009; LUCA.
DR   HOGENOM; HOG000076160; -.
DR   KO; K07566; -.
DR   OMA; GMLKSHY; -.
DR   OrthoDB; 1913202at2; -.
DR   BioCyc; RPOM246200:G1G48-302-MONOMER; -.
DR   Proteomes; UP000001023; 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:UniProtKB-UniRule.
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; IPR005145; SUA5.
DR   InterPro; IPR038385; Sua5/YwlC_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   3: Inferred from homology;
DR   PRODOM; Q5LX83.
DR   SWISS-2DPAGE; Q5LX83.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR004930,
KW   ECO:0000256|PIRSR:PIRSR004930-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR004930};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004930,
KW   ECO:0000256|PIRSR:PIRSR004930-1};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004930};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004930};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR004930}.
FT   DOMAIN       13    199       YrdC-like. {ECO:0000259|PROSITE:PS51163}.
FT   BINDING      35     35       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING      58     58       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      62     62       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      67     67       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     118    118       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     122    122       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     142    142       L-threonine; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     144    144       ATP; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     152    152       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     182    182       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     195    195       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     231    231       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
SQ   SEQUENCE   316 AA;  32718 MW;  6F19229B4D38DF39 CRC64;
     MPVQPTLRLA ADPDGIARAA ELLRDGRLVA FPTETVYGLG GDATNGQAVA GIYAAKGRPS
     FNPLIAHVAS AEAARRHVHW SETAERLATA FWPGPLTLVL PLRANHGISE LVTAGLDTLA
     VRVPAHPTAR TLLATLDRPV AAPSANPSGR ISPTTADHVL AGLDGRIAAV LDAGPCGVGV
     ESTIVGLSGT PILLRPGGLP TEEIEALLGQ PLARHQQGDN ISAPGQLLSH YAPQSTVRLN
     ARAPSDGEVF LGFGPMDCDE NLSPSGNLTE AAANLFAALH RLDTTGKPIA IAPIPERGLG
     LAINDRLRRA AAPRDP
//

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