TMCA_HAEIN
ID TMCA_HAEIN Reviewed; 656 AA.
AC P44140; P44141; P44142;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
GN Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886};
GN OrderedLocusNames=HI_1254/HI_1255/HI_1256;
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 formation of N(4)-acetylcytidine (ac(4)C) at
CC the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC donor and ATP (or GTP). {ECO:0000255|HAMAP-Rule:MF_01886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O =
CC ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) +
CC phosphate; Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC EC=2.3.1.193; Evidence={ECO:0000255|HAMAP-Rule:MF_01886};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
CC -!- CAUTION: Could be the product of a pseudogene. Three frameshifts
CC produce three separate ORFs. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22904.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC22910.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC22911.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22904.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L42023; AAC22910.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L42023; AAC22911.1; ALT_FRAME; Genomic_DNA.
DR PIR; E64023; E64023.
DR PIR; F64023; F64023.
DR PIR; G64023; G64023.
DR AlphaFoldDB; P44140; -.
DR SMR; P44140; -.
DR STRING; 71421.HI_1254; -.
DR EnsemblBacteria; AAC22904; AAC22904; HI_1254.
DR EnsemblBacteria; AAC22910; AAC22910; HI_1255.
DR EnsemblBacteria; AAC22911; AAC22911; HI_1256.
DR KEGG; hin:HI_1254; -.
DR KEGG; hin:HI_1255; -.
DR KEGG; hin:HI_1256; -.
DR eggNOG; COG1444; Bacteria.
DR HOGENOM; CLU_784735_0_0_6; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0051392; F:tRNA N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0051391; P:tRNA acetylation; IBA:GO_Central.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IBA:GO_Central.
DR Gene3D; 1.20.120.890; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR007807; Helicase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032672; TmcA/NAT10/Kre33.
DR InterPro; IPR038321; TmcA_C_sf.
DR InterPro; IPR033442; TmcA_tRNA_bind.
DR InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
DR Pfam; PF13718; GNAT_acetyltr_2; 2.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF17176; tRNA_bind_3; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 5: Uncertain;
KW Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..656
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000013891"
FT DOMAIN 368..542
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 167..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 474..476
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 481..487
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 510
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 656 AA; 75162 MW; 9975F7685CB45303 CRC64;
MPSRQLQILI RKTLPLVPDH VLIIGESGIA FSKATNLLGQ EFEHILFDGR NGIHLEALAI
AAGTLKMGGT LCLVLSDWEN LSQQPDQDSL RWNGNQSAIA TPNFIYHFKQ CIERYHFPIL
REESAVEFPT VFYSNEHHKN ATLAQQQIIE NILQAEQDIY FLTAKRGRGK SALLGMLANQ
IQAPVYLTAP NKSAVHSVIE FSEGDIEFIA PDELALTLQT EPEFSQSAWL LVDEAAMIPL
PLLQEYSRYF QHIVFSTTIH SYEGTGRGFE LKFKRKIHRT FQHFELKQPL RWQENDPLEH
FIDDLLLLNA EDDFQHFDYS NITYNIEENA KNLSFPCLRG KVPEGPKGDL DIASLPQALE
ALLTSKGSEG KYNRQFFFRD FYGLMTIAHY RTSPLDLRRL LDGKNQRFYF AEYQQNLLGA
IWALEEGNMA DDELIIQIQQ GKRRPKGNLV PQALCFHENL SQACKLRSLR ISRIAVQPNW
QQKGIGQNLM QAMENADVDF LSVSFGYTDE LAKFWQKCGF VLVHLGEHQE ASSGCYSAIA
LKGISKEGLA LVDTAYKQFQ RNLPLSFHPF AINFEQNQLD WQLDDFDWMS LKNFANFHRT
LFSSIPAMRR LLKLAGKENF PLISAYLTKK QFPINKKKGV ECLRLEIKQY LERGTL
