(data stored in SCRATCH zone)

SWISSPROT: C3MIA0_SINFN

ID   C3MIA0_SINFN            Unreviewed;       337 AA.
AC   C3MIA0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
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=NGR_c06550 {ECO:0000313|EMBL:ACP24448.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24448.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24448.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: L-threonine + ATP + HCO(3)(-) = L-
CC       threonylcarbamoyladenylate + diphosphate + H(2)O.
CC       {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; CP001389; ACP24448.1; -; Genomic_DNA.
DR   RefSeq; WP_012707233.1; NC_012587.1.
DR   RefSeq; YP_002825201.1; NC_012587.1.
DR   STRING; 394.NGR_c06550; -.
DR   EnsemblBacteria; ACP24448; ACP24448; NGR_c06550.
DR   GeneID; 7791881; -.
DR   KEGG; rhi:NGR_c06550; -.
DR   PATRIC; fig|394.7.peg.3468; -.
DR   eggNOG; ENOG4107QIS; Bacteria.
DR   eggNOG; COG0009; LUCA.
DR   HOGENOM; HOG000076160; -.
DR   KO; K07566; -.
DR   OMA; NCIVEIV; -.
DR   OrthoDB; POG091H00HZ; -.
DR   Proteomes; UP000001054; 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; 3.90.870.10; -; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR005145; SUA5.
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; C3MIA0.
DR   SWISS-2DPAGE; C3MIA0.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR004930,
KW   ECO:0000256|PIRSR:PIRSR004930-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:UP000001054};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004930};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR004930}.
FT   DOMAIN       10    195       YrdC-like. {ECO:0000259|PROSITE:PS51163}.
FT   BINDING      32     32       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING      55     55       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      59     59       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      64     64       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     114    114       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     118    118       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     137    137       L-threonine; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     139    139       ATP; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     147    147       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     177    177       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     191    191       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     227    227       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
SQ   SEQUENCE   337 AA;  35154 MW;  631C3DF1E9542850 CRC64;
     MIIDVAADPA AGITSAVEAL GRGDVIAVPT ETVYGLAADA TNEAAVSQIF DIKRRPGFNP
     LICHCSDLEM VSEFATLDPV SLRLAERFWP GPMTLVLNSN PGRLPSVTTA GLTTVAIRIP
     MGFSNGLIRS YGGPLAAPSA NISGRVSATT AAHVESEFGD GVPLILDGGP TKIGVESTIL
     RVRENGIELL RPGGLPIELV EHAAGLQVSA PNLFRKVLAP GMLTSHYAPR AMVRLNATGV
     GPGETLLKFG DAIVPGEGAC ARVFNLSPEG SLEEFAAKLY ATLKEADDAG AESIAIVPIP
     DEGLGLAIND RLRRAAAPRT LTLGELEQAA VRNREAR
//

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