(data stored in ACNUC7421 zone)

SWISSPROT: D1CDG0_THET1

ID   D1CDG0_THET1            Unreviewed;       335 AA.
AC   D1CDG0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 61.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000256|HAMAP-Rule:MF_01445};
GN   OrderedLocusNames=Tter_0043 {ECO:0000313|EMBL:ACZ40966.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40966.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40966.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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. Is involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC       N6 group of A37, together with TsaE and TsaB. TsaD likely plays a
CC       direct catalytic role in this reaction. {ECO:0000256|HAMAP-
CC       Rule:MF_01445, ECO:0000256|SAAS:SAAS00946755}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate =
CC         AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-
CC         COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215;
CC         EC=2.3.1.234; Evidence={ECO:0000256|HAMAP-Rule:MF_01445,
CC         ECO:0000256|SAAS:SAAS01118598};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445,
CC       ECO:0000256|SAAS:SAAS00946736}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01445, ECO:0000256|SAAS:SAAS00946735}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01445}.
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DR   EMBL; CP001825; ACZ40966.1; -; Genomic_DNA.
DR   RefSeq; WP_012874001.1; NC_013525.1.
DR   STRING; 525904.Tter_0043; -.
DR   EnsemblBacteria; ACZ40966; ACZ40966; Tter_0043.
DR   KEGG; ttr:Tter_0043; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 1257362at2; -.
DR   BioCyc; TTER525904:G1GGS-43-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
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; 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; TIGR03723; T6A_TsaD_YgjD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDG0.
DR   SWISS-2DPAGE; D1CDG0.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00946739};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00946752};
KW   Hydrolase {ECO:0000313|EMBL:ACZ40966.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01445, ECO:0000256|SAAS:SAAS00946733};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00946748};
KW   Protease {ECO:0000313|EMBL:ACZ40966.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00946732};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01445,
KW   ECO:0000256|SAAS:SAAS00946749}.
FT   DOMAIN       26    306       Peptidase_M22. {ECO:0000259|Pfam:
FT                                PF00814}.
FT   REGION      140    144       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01445}.
FT   METAL       111    111       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   METAL       115    115       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   METAL       300    300       Iron. {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   BINDING     173    173       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01445}.
FT   BINDING     186    186       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01445}.
FT   BINDING     275    275       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01445}.
SQ   SEQUENCE   335 AA;  36062 MW;  0BA0B2D6D535B61D CRC64;
     MNILAIETSC DETSAAVIAD GYLVKSNIVA SQIDIHRRFG GVFPEVASRQ HVLAILPTIE
     ESLSKAQVGW EDIDAIAVTK GPGLVGSLLV GVNTAKGIAW ARDLPLIGSN HIEGHIYANW
     LQEDPNAPRH IPQFPLLALI VSGGHTELIL MKDHGVYERL GRTLDDAAGE AFDKAARILG
     LGFPGGPAIQ KAAEKAEGRE FVLPRAELPG TFNFSFSGLK TALLRAVESS ENVDVYALAN
     GFQESVVDIL VRKTVAAAEQ TAAKEVVIAG GVAANTRLRE RIKQELGEKV RVPKFEYCTD
     NAAMIGGLAY YRYIRGKTDQ LDLDVDPNLD LVVDA
//

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