MNMC_YERPE
ID MNMC_YERPE Reviewed; 689 AA.
AC Q8ZD36; Q0WDD5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000255|HAMAP-Rule:MF_01102};
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=2.1.1.61 {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=1.5.-.- {ECO:0000255|HAMAP-Rule:MF_01102};
GN Name=mnmC {ECO:0000255|HAMAP-Rule:MF_01102};
GN OrderedLocusNames=YPO2756, y1590, YP_2407;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01102};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM85159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21375.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85159.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62612.1; -; Genomic_DNA.
DR PIR; AD0336; AD0336.
DR RefSeq; WP_002209716.1; NZ_WHLN01000016.1.
DR RefSeq; YP_002347703.1; NC_003143.1.
DR PDB; 3PVC; X-ray; 2.31 A; A=1-689.
DR PDB; 3SGL; X-ray; 2.70 A; A=1-689.
DR PDBsum; 3PVC; -.
DR PDBsum; 3SGL; -.
DR AlphaFoldDB; Q8ZD36; -.
DR SMR; Q8ZD36; -.
DR IntAct; Q8ZD36; 4.
DR STRING; 214092.YPO2756; -.
DR PaxDb; Q8ZD36; -.
DR EnsemblBacteria; AAM85159; AAM85159; y1590.
DR EnsemblBacteria; AAS62612; AAS62612; YP_2407.
DR GeneID; 57975933; -.
DR KEGG; ype:YPO2756; -.
DR KEGG; ypk:y1590; -.
DR KEGG; ypm:YP_2407; -.
DR PATRIC; fig|1028802.3.peg.1489; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_2_1_6; -.
DR OMA; NFLCAWQ; -.
DR BRENDA; 2.1.1.229; 4559.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.50.50.60; -; 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; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05430; Methyltransf_30; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..689
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000095033"
FT REGION 1..245
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 270..689
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 42..49
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3SGL"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 321..342
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 473..477
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 481..491
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 536..549
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 566..573
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 587..593
FT /evidence="ECO:0007829|PDB:3PVC"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:3SGL"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 617..625
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 631..646
FT /evidence="ECO:0007829|PDB:3PVC"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:3SGL"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:3PVC"
FT HELIX 665..671
FT /evidence="ECO:0007829|PDB:3PVC"
SQ SEQUENCE 689 AA; 76671 MW; 84812EC4DE06A2D4 CRC64;
MNQRPIQTAT LSWNEQGTPV SEQFGDIYFS NEDGLEETHH VFLKGNGFPA RFASHPQQSC
IFAETGFGTG LNFLTLWRDF ALFRQQSPNA TLRRLHYISF EKYPLHVADL ASAHARWPEL
ASFAEQLRAQ WPLPLAGCHR ILLADGAITL DLWFGDVNTL LPTLDDSLNN QVDAWFLDGF
APAKNPDMWN EQLFNAMARM TRPGGTFSTF TAAGFVRRGL QQAGFNVTKV KGFGQKREML
TGTLPQQIHA PTAPWYHRPA ATRCDDIAII GGGIVSALTA LALQRRGAVV TLYCADAQPA
QGASGNRQGA LYPLLNGKND ALETFFTSAF TFARRQYDQL LEQGIAFDHQ WCGVSQLAFD
DKSRGKIEKM LHTQWPVEFA EAMSREQLSE LAGLDCAHDG IHYPAGGWLC PSDLTHALMM
LAQQNGMTCH YQHELQRLKR IDSQWQLTFG QSQAAKHHAT VILATGHRLP EWEQTHHLPL
SAVRGQVSHI PTTPVLSQLQ QVLCYDGYLT PVNPANQHHC IGASYQRGDI ATDFRLTEQQ
ENRERLLRCL PQVSWPQQVD VSDNQARCGV RCAIRDHLPM VGAVPDYAAT LAQYQDLSRR
IQHGGESEVN DIAVAPVWPE LFMVGGLGSR GLCSAPLVAE ILAAQMFGEP LPLDAKTLAA
LNPNRFWIRK LLKGRPVQTR SPATQESSR
