(data stored in ACNUC30630 zone)

SWISSPROT: TSAD_CORGB

ID   TSAD_CORGB              Reviewed;         344 AA.
AC   A4QBT6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=cgR_0712;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF53683.1; -; Genomic_DNA.
DR   RefSeq; WP_011896813.1; NC_009342.1.
DR   SMR; A4QBT6; -.
DR   EnsemblBacteria; BAF53683; BAF53683; cgR_0712.
DR   KEGG; cgt:cgR_0712; -.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   BioCyc; CGLU340322:G1G2L-752-MONOMER; -.
DR   Proteomes; UP000006698; 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; 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.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4QBT6.
DR   SWISS-2DPAGE; A4QBT6.
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase;
KW   tRNA processing.
FT   CHAIN           1..344
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000303339"
FT   REGION          135..139
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           113
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           117
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   METAL           306
FT                   /note="Iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         169
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         182
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         278
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   344 AA;  35801 MW;  60BA564777D83778 CRC64;
     MIVLGIESSC DETGVGVVKL DGEGNLEILA DSVASSMQEH ARFGGVVPEI ASRAHLESMV
     PVMREALRQA GVDKPDAVAA TVGPGLAGAL LVGASAAKAY AAAWGVPFYA VNHLGGHVAV
     ANLEGETLPH AVALLVSGGH TQLLEVDAVG LPMKELGSTL DDAAGEAYDK VSRLLGLGYP
     GGPIIDKLAR RGNPEAIAFP RGLMKKSDSR HDFSFSGLKT SVARYVEAAE RNGEVISVED
     VCASFQEAVC DVLTFKAVRA CRDVGAKVLL LGGGVAANSR LRELAQERCD KAGIELRVPR
     FNLCTDNGVM IAALAAQRIH EGAQESPISV GTDPSLSVET PQVF
//

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