TMCAL_THEMA
ID TMCAL_THEMA Reviewed; 418 AA.
AC Q9X1K1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000255|HAMAP-Rule:MF_01539};
DE EC=6.3.4.- {ECO:0000255|HAMAP-Rule:MF_01539};
GN Name=tmcAL {ECO:0000255|HAMAP-Rule:MF_01539}; OrderedLocusNames=TM_1513;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC the wobble position of elongator tRNA(Met), using acetate and ATP as
CC substrates. First activates an acetate ion to form acetyladenylate (Ac-
CC AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
CC {ECO:0000255|HAMAP-Rule:MF_01539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP +
CC diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met);
CC Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA-COMP:10694,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01539};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01539}.
CC -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000255|HAMAP-
CC Rule:MF_01539}.
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DR EMBL; AE000512; AAD36580.1; -; Genomic_DNA.
DR PIR; B72245; B72245.
DR RefSeq; NP_229313.1; NC_000853.1.
DR PDB; 5Y0R; X-ray; 3.11 A; A=1-418.
DR PDB; 5Y0S; X-ray; 2.10 A; A/B/C/D=1-418.
DR PDB; 5Y0T; X-ray; 1.90 A; A/B/C/D=1-418.
DR PDBsum; 5Y0R; -.
DR PDBsum; 5Y0S; -.
DR PDBsum; 5Y0T; -.
DR AlphaFoldDB; Q9X1K1; -.
DR SMR; Q9X1K1; -.
DR STRING; 243274.THEMA_06735; -.
DR EnsemblBacteria; AAD36580; AAD36580; TM_1513.
DR KEGG; tma:TM1513; -.
DR eggNOG; COG1323; Bacteria.
DR InParanoid; Q9X1K1; -.
DR OMA; WARTKMA; -.
DR OrthoDB; 1547014at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01539; TmcAL; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase.
DR PANTHER; PTHR37825; PTHR37825; 1.
DR Pfam; PF05636; HIGH_NTase1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome; RNA-binding; tRNA processing; tRNA-binding.
FT CHAIN 1..418
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_0000147197"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 374..392
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:5Y0T"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5Y0T"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5Y0T"
SQ SEQUENCE 418 AA; 48592 MW; 60C1196BE5C933C1 CRC64;
MEYNPFHNGH LYHLTSAREL VKPDYTIAVM SGNFCQRGEP AVIDKFARAE IALRMGVDVV
LELPVVFATQ DAGGFAFGAV CVLDATGVVT DVVFGSESND IEFLQRVARI LYEQPDEYQK
FLHEELKKGY SFPNARKYAL MRYFSMKGWN EEEVLKLEKS NDILGVEYIH SALKIGSNIR
FHTIKRVGAE EKDTSFRGRF SSATAIRNLM REKRWEEVRD SLPEDSFEIL MREINEGRGP
VFLENMGDFL LSFFRLKNMD FFEKIHGFSE GLEKRFHVCA RQTGSYRDFL ECVKAKRFTF
SRIRRLALFS VFEVNKEFVE KSNTKGPQYI RILGFTEKGR EILSLMRKKA KLPIVTNMSL
YRKVLEKTDL PVDKQLFLEQ IDLDVKATNF YSMFFPSVEQ RCGERDFSIH PIFLRTEM
