(data stored in ACNUC7421 zone)

SWISSPROT: C3MHF1_SINFN

ID   C3MHF1_SINFN            Unreviewed;       324 AA.
AC   C3MHF1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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_c04830 {ECO:0000313|EMBL:ACP24279.1};
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:ACP24279.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24279.1, 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; ACP24279.1; -; Genomic_DNA.
DR   RefSeq; WP_012707064.1; NC_012587.1.
DR   RefSeq; YP_002825032.1; NC_012587.1.
DR   STRING; 394.NGR_c04830; -.
DR   EnsemblBacteria; ACP24279; ACP24279; NGR_c04830.
DR   GeneID; 7791709; -.
DR   KEGG; rhi:NGR_c04830; -.
DR   PATRIC; fig|394.7.peg.3291; -.
DR   eggNOG; ENOG4107QIS; Bacteria.
DR   eggNOG; COG0009; LUCA.
DR   HOGENOM; HOG000076160; -.
DR   KO; K07566; -.
DR   OMA; GMLKSHY; -.
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; C3MHF1.
DR   SWISS-2DPAGE; C3MHF1.
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       12    198       YrdC-like. {ECO:0000259|PROSITE:PS51163}.
FT   BINDING      34     34       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING      57     57       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      61     61       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING      66     66       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     117    117       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     121    121       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     140    140       L-threonine; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     142    142       ATP; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     150    150       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     180    180       L-threonine. {ECO:0000256|PIRSR:
FT                                PIRSR004930-1}.
FT   BINDING     194    194       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
FT   BINDING     231    231       ATP. {ECO:0000256|PIRSR:PIRSR004930-1}.
SQ   SEQUENCE   324 AA;  33814 MW;  23F441CFEA7EED5B CRC64;
     MAEIIDTRIE PDRAIEKACA ALSEGEPVAI PTETVYGLAA DATNADAISR IYEMKGRPRF
     NPLICHVSDM AMAEAHVVFD PLSRRLAEAF WPGPLTLILP ERRESTVHAL ASAGLETLGI
     RMPEGFSRRV ISHFGRPLAA PSANTSGKIS PTSAAHVEAD LGAKLGLILD AGPAEIGLES
     TIIKVEAGRL RLLRPGGLDA AEIEALTGLT VGRPEAAGAT IEAPGMLASH YAPGAAVRLN
     AKDVRKGEAL IRFGGKALPG ESAAAIVLDL SPSGNLREAA ANLFDYMKRA DASGVSSIAF
     GPVPSEGLGE AIVDRLERAA APRI
//

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