(data stored in SCRATCH3701 zone)

SWISSPROT: TSAD_RICTY

ID   TSAD_RICTY              Reviewed;         387 AA.
AC   Q68XR3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp;
GN   OrderedLocusNames=RT0093;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaE and TsaB. TsaD likely plays a direct catalytic role
CC       in this reaction. {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
DR   EMBL; AE017197; AAU03579.1; -; Genomic_DNA.
DR   RefSeq; WP_011190566.1; NC_006142.1.
DR   SMR; Q68XR3; -.
DR   STRING; 257363.RT0093; -.
DR   EnsemblBacteria; AAU03579; AAU03579; RT0093.
DR   KEGG; rty:RT0093; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 1257362at2; -.
DR   BioCyc; RTYP257363:G1G0L-96-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR022437; RPE3.
DR   InterPro; IPR022450; TsaD.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR   TIGRFAMs; TIGR03775; RPE3; 1.
DR   TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68XR3.
DR   SWISS-2DPAGE; Q68XR3.
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase;
KW   tRNA processing.
FT   CHAIN           1..387
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000303525"
FT   REGION          134..138
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           112
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           116
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           353
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         167
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         180
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         325
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   387 AA;  42546 MW;  E29017BB64063847 CRC64;
     MKKILGIESS CDDTAISIIT ESRKILSNII IPQNTEHAVF GGVVPEIAAR SHLSNLDQAL
     ENVLTKSNTE LTEISAIAAT SGPGLIGGVI VGSMFARSLS SALNKPFIAI NHLEGHALTV
     RLTDNISYPY LLLLASGGHC QFVAVLGLGK YKILGSTIDD AIGETFDKVA KMLNLSFPGG
     PEIEKRAKLG NPHKYKFPKP IINSGNCNMS FSGLKTAVRN LIMSLKEVND SVINDIAASF
     QFTIGAILSS KMLNAIRLYQ QILNYYYENV DYTTNLNLKS FRQDEFNLNH LQDITRPKSR
     IYLQNSFRSN LLNDTIVIAG GVAANKYLQE ILSNCTQTYG YRLIAPPMHL CTDNAAMIAY
     AGLERYNNKL FSPLNFCPKA KWSLEDI
//

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