ID TSAD_SYNP2 Reviewed; 355 AA.
AC B1XJF0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 02-NOV-2016, entry version 65.
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=SYNPCC7002_A1007;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC Rule:MF_01445}.
CC -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in
CC tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
CC {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-
CC 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; CP000951; ACA99010.1; -; Genomic_DNA.
DR RefSeq; WP_012306634.1; NC_010475.1.
DR ProteinModelPortal; B1XJF0; -.
DR STRING; 32049.SYNPCC7002_A1007; -.
DR EnsemblBacteria; ACA99010; ACA99010; SYNPCC7002_A1007.
DR KEGG; syp:SYNPCC7002_A1007; -.
DR PATRIC; 23816536; VBISynSp37135_1224.
DR eggNOG; ENOG4105CPM; Bacteria.
DR eggNOG; COG0533; LUCA.
DR HOGENOM; HOG000109568; -.
DR KO; K01409; -.
DR OMA; ICIDHIL; -.
DR OrthoDB; POG091H010B; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-HAMAP.
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; IPR022450; TsaD.
DR Pfam; PF00814; Peptidase_M22; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1 355 tRNA N6-adenosine
FT threonylcarbamoyltransferase.
FT /FTId=PRO_1000146033.
FT REGION 134 138 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_01445}.
FT METAL 111 111 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT METAL 115 115 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT METAL 307 307 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT BINDING 167 167 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01445}.
FT BINDING 180 180 Substrate; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_01445}.
FT BINDING 184 184 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01445}.
FT BINDING 279 279 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01445}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 96 116 ipat:GLYCOPROTEASE [T]
FT MYHIT 23 313 ipfam:Peptidase_M22 [T]
FT MYHIT 2 338 ihamap:TsaD [T]
SQ SEQUENCE 355 AA; 37613 MW; DAC16FAD876F1853 CRC64;
MSIVLAIETS CDETAVAIVN NRKVLGNVVA SQIDIHREFG GVVPEVASRH HLESINACID
TAFEQSGLSW SEIEAIATTC APGLVGALLL GAAAGKTLAM IHNKPFIGVH HLEGHIYASY
LSQPELEPPF LCLLVSGGHT SFIEVRGCGE YKLLGETRDD AAGEAFDKVA RLLRVGYPGG
PVIDRLAKTG DPQAFKLPEG RISLPGGGYH PYDCSFSGLK TAVLRLVQQF ETQGKAVPVA
DIAASFQYTV AQALTKRAVR CAGDRQLQTI VVGGGVAANS GLRQILTAAA AEAGIQVYFP
PLKFCTDNAA MIACAAAEHF QKGDRSRLDL PVASRLPITQ VQTLYTPLVP LKGKS
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