(data stored in ACNUC7421 zone)

SWISSPROT: TSAD_STRM5

ID   TSAD_STRM5              Reviewed;         341 AA.
AC   B4SHI9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=Smal_0327;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-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:
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: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; CP001111; ACF50032.1; -; Genomic_DNA.
DR   RefSeq; WP_012509844.1; NC_011071.1.
DR   SMR; B4SHI9; -.
DR   STRING; 391008.Smal_0327; -.
DR   PRIDE; B4SHI9; -.
DR   EnsemblBacteria; ACF50032; ACF50032; Smal_0327.
DR   KEGG; smt:Smal_0327; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 1257362at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01710-MONOMER; -.
DR   Proteomes; UP000001867; 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; 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; B4SHI9.
DR   SWISS-2DPAGE; B4SHI9.
KW   Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW   Transferase; tRNA processing.
FT   CHAIN         1    341       tRNA N6-adenosine
FT                                threonylcarbamoyltransferase.
FT                                /FTId=PRO_1000146026.
FT   REGION      138    142       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   METAL       115    115       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       119    119       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       304    304       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     171    171       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   BINDING     184    184       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     276    276       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
SQ   SEQUENCE   341 AA;  35844 MW;  DD6DACE8A28DE9ED CRC64;
     MRVLGIESSC DETGVAVYDT DLAGSAALRA HAVYSQIALH AEYGGVVPEL ASRDHVRKLL
     PLVRQTLAEA GLGVGDIDGV AYTAGPGLVG ALLVGAGVAR SLAWALEVPA VGVHHMEGHL
     LAPLMEDDPP QAPFVALLVS GGHTQLVAVD AIGQYRLLGE TLDDAAGEAF DKTAKMMGLP
     YPGGPQLARL AEQGTPGVYR FARPMIDRPG LDFSFSGLKT QVLMAWRDSD QSEQTRADIA
     RGFEDAVVET LSIKCERALE AAGTNVIVVA GGVGANKRLR ARLQQMAERL GGRACFPRPA
     LCTDNGAMIA FAGALRLQAG QHSPPKVDVT PRWDMATLPA V
//

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