ID A0A0W0Y765_9GAMM Unreviewed; 673 AA.
AC A0A0W0Y765;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|HAMAP-Rule:MF_01102};
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000256|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102};
DE EC=2.1.1.61 {ECO:0000256|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102};
DE EC=1.5.-.- {ECO:0000256|HAMAP-Rule:MF_01102};
GN Name=mnmC_3 {ECO:0000313|EMBL:KTD52430.1};
GN Synonyms=mnmC {ECO:0000256|HAMAP-Rule:MF_01102};
GN ORFNames=Lrub_0062 {ECO:0000313|EMBL:KTD52430.1};
OS Legionella rubrilucens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD52430.1, ECO:0000313|Proteomes:UP000054608};
RN [1] {ECO:0000313|EMBL:KTD52430.1, ECO:0000313|Proteomes:UP000054608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD52430.1,
RC ECO:0000313|Proteomes:UP000054608};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position
CC (U34) in tRNA. Catalyzes the FAD-dependent demodification of
CC cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl
CC group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC mnm(5)s(2)U34. {ECO:0000256|HAMAP-Rule:MF_01102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569, Rhea:RHEA-
CC COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454,
CC ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01102};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000256|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_01102}.
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:KTD52430.1}.
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DR EMBL; LNYT01000001; KTD52430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0Y765; -.
DR STRING; 458.Lrub_0062; -.
DR PATRIC; fig|458.5.peg.63; -.
DR Proteomes; UP000054608; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01102; MnmC; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008471; MnmC-like_methylTransf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR InterPro; IPR047785; tRNA_MNMC2.
DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR NCBIfam; TIGR03197; MnmC_Cterm; 1.
DR NCBIfam; NF033855; tRNA_MNMC2; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF283; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05430; Methyltransf_30; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01102};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01102};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01102}; Reference proteome {ECO:0000313|Proteomes:UP000054608};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01102};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01102}.
FT DOMAIN 118..251
FT /note="MnmC-like methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05430"
FT DOMAIN 279..635
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 1..253
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
FT REGION 282..673
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01102"
SQ SEQUENCE 673 AA; 75058 MW; F95977F53EFF5B17 CRC64;
MSSPFTVIQM ADLQWQEGLP YSPAFDDVYF SREDGFAEKQ YVFIEGNCLR ERLTRLHEQE
NPLFTIAETG FGTGLNFLLT WQFWQNHAPQ NARLFYFSCE KFPLKKEDLE ACLQLWPPLQ
AFSQQLLEEY PVLTPGFHRL TFDQGRIHLI LMLGDAQHCF DELLLSGDRE LDRALSHTAV
DAWYLDGFSP RRNERMWTHS LFQTMALLSR PGTTVATYSA AAQVKAGLEA SGFSLTKKPG
YGRKRHMLTA ELAEASQSKR RRQTPWFYTP GSMREKRRAI IVGAGLAGCF CAHALSRRGW
QVQLFDEAPQ AAAGASGNER AVVYPRLSAY RSPLTEFMLA AFLYAQAFYK RVAGVDVEGD
MQGILQLACN TRELKAQRSM RDWLLAYPQL AMPVSAAEAS ELAGLTLEFS GLFIPLSGWL
NSRELCLYLL QQSPQVQWFG QTTVMEMQIE GGQWHVNGQE ADVVIVTTGF RANQFAQTAG
LPIKPIGGQI TFVQAQAASA GLTLPLCGEG HVLPAKNNLH ALGATYHLNQ PRARCCSEDD
STNLQKISPM ASELQFYRDG IVRSWAGVRG ATPDYLPLVG AVPVEDEFLA CYAGLDSHAE
RWIKVPPPVY PGLYVCAGFG SRGLTTIPLS AEWLAGQISG EPGFFSRSMM KAVSPSRFLL
RQIIRSRQAQ AEE
//
