TCDA_HAEIN
ID TCDA_HAEIN Reviewed; 261 AA.
AC Q57097; O05009;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=tRNA threonylcarbamoyladenosine dehydratase;
DE EC=6.1.-.-;
DE AltName: Full=t(6)A37 dehydratase;
GN Name=tcdA; OrderedLocusNames=HI_0118;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the ATP-dependent dehydration of
CC threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic
CC t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC21793.1; -; Genomic_DNA.
DR PIR; C64049; C64049.
DR RefSeq; NP_438290.1; NC_000907.1.
DR AlphaFoldDB; Q57097; -.
DR SMR; Q57097; -.
DR STRING; 71421.HI_0118; -.
DR EnsemblBacteria; AAC21793; AAC21793; HI_0118.
DR KEGG; hin:HI_0118; -.
DR PATRIC; fig|71421.8.peg.122; -.
DR eggNOG; COG1179; Bacteria.
DR HOGENOM; CLU_013325_4_0_6; -.
DR OMA; DMDDICV; -.
DR PhylomeDB; Q57097; -.
DR BioCyc; HINF71421:G1GJ1-128-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061503; F:tRNA threonylcarbamoyladenosine dehydratase; IBA:GO_Central.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0061504; P:cyclic threonylcarbamoyladenosine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; PTHR43267; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..261
FT /note="tRNA threonylcarbamoyladenosine dehydratase"
FT /id="PRO_0000120580"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 28572 MW; 6829BCBFFB2C81F0 CRC64;
MGITVMARID NYEQRFGGIG RLYTPDSLAR LRQAHICVIG IGGVGSWVVE ALARSGIGEL
TLIDMDDICV TNINRQLPAM SGTIGKLKTE VMSERVKLIN PECTVNIIDD FISPENQSDY
LNRGYDYVID AIDNVKTKAS LIAYCKRNKI NVITIGGAGG QTDPTQIQIA DLSKTIQDPL
LAKVRSVLRK DYNFSQNPKR KFSIDAVFST QPLIFPQMTE GCSTSATMNC ANGFGAATMI
TATFGFFAVS RVIDKLLKKK S