ID G9Z610_9ENTR Unreviewed; 375 AA.
AC G9Z610;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000256|HAMAP-Rule:MF_01012};
DE EC=2.1.1.189 {ECO:0000256|HAMAP-Rule:MF_01012};
DE AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01012};
GN Name=rlmC {ECO:0000256|HAMAP-Rule:MF_01012};
GN ORFNames=HMPREF0880_02802 {ECO:0000313|EMBL:EHM47057.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM47057.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM47057.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM47057.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC (m5U747) in 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01012};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01012}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM47057.1}.
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DR EMBL; AGCL01000039; EHM47057.1; -; Genomic_DNA.
DR RefSeq; WP_006819254.1; NZ_JH417874.1.
DR AlphaFoldDB; G9Z610; -.
DR STRING; 1002368.HMPREF0880_02802; -.
DR PATRIC; fig|1002368.3.peg.2552; -.
DR HOGENOM; CLU_014689_0_0_6; -.
DR Proteomes; UP000003044; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1.
DR InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR02085; meth_trns_rumB; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01012};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01012};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01012}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01012};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01012}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01012};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01012};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01012}.
FT ACT_SITE 334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 3
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01012,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 375 AA; 41742 MW; 93A820B7BB2B562B CRC64;
MQCALYDADR CRSCQWITRP VSDQLSAKMD DLRQLLAEMP VGEWCAPVSG PEQGFRNKAK
MVVSGSVEKP LLGMLHRDGT PEDLTDCPLY PDSFAPVFAV LKPFIARAGL TPYNVARKRG
ELKYVLLTES QRDGGMMLRF VLRSHSKIAQ LRAALPWLQA QLPQLKVITA NIQPVHMAIM
EGEEEIYFTG QQALGETLND VPLWIRPQSF FQTNPTVAAR LYATAREWVC GLPVQHMWDL
FCGVGGFGLH CATPEMKLTG IEIAPEAIAC AKQSAAELGL TNLHFQALDS TQFATGQGEV
PELVLVNPPR RGIGKALCDY LSEMAPPYII YSSCNAQTMA KDIAHLPGYR VERVQLFDLF
PHTAHYEVLT LLIRR
//
