MNMA_MYCGA
ID MNMA_MYCGA Reviewed; 657 AA.
AC Q7NBZ0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Trifunctional protein RibF/MnmA;
DE Includes:
DE RecName: Full=FMN adenylyltransferase;
DE EC=2.7.7.2;
DE AltName: Full=FAD pyrophosphorylase;
DE AltName: Full=FAD synthase;
DE Includes:
DE RecName: Full=Riboflavin kinase;
DE EC=2.7.1.26;
DE AltName: Full=Flavokinase;
DE Includes:
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE EC=2.8.1.13;
GN Name=ribF/mnmA; OrderedLocusNames=MYCGA1200; ORFNames=MGA_0832;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
CC -!- FUNCTION: Involved in FAD and FMN biosynthesis. {ECO:0000250}.
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC ChEBI:CHEBI:456215; EC=2.8.1.13;
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RibF family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MnmA/TRMU family.
CC {ECO:0000305}.
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DR EMBL; AE015450; AAP56470.1; -; Genomic_DNA.
DR RefSeq; WP_011113349.1; NC_004829.2.
DR AlphaFoldDB; Q7NBZ0; -.
DR SMR; Q7NBZ0; -.
DR KEGG; mga:MGA_0832; -.
DR PATRIC; fig|233150.7.peg.134; -.
DR HOGENOM; CLU_417276_0_0_14; -.
DR OMA; VSCELEN; -.
DR OrthoDB; 1054741at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd02064; FAD_synthetase_N; 1.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 2.40.30.30; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR002606; Riboflavin_kinase_bac.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR Pfam; PF06574; FAD_syn; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF82114; SSF82114; 1.
DR TIGRFAMs; TIGR00083; ribF; 1.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Disulfide bond; FAD; Flavoprotein; FMN; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..657
FT /note="Trifunctional protein RibF/MnmA"
FT /id="PRO_0000349871"
FT REGION 1..141
FT /note="FMN adenylyltransferase"
FT REGION 158..282
FT /note="Riboflavin kinase"
FT REGION 283..657
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT REGION 389..391
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 442..444
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 492
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 292..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 421
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 635
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 394..492
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 75974 MW; C2F795910B8821EF CRC64;
MLSIINLTSK TIKEVNKGVD LVIGFFDGIH KGHAKLFKQS DRFNLLTFDH IPKKQRLLYP
KVDEIEQLSA LSGLEQLLVY DLLNNNLSAQ EFIDNYIKLI QPKRIIVGSD FKFGSDQVDY
SLFAKNGYEV VVVKKDHCST SEIKKLIINC DLDQANKLLL TPFYLKGTVI KNAQRGRTIG
FVTANIILDN QLIELTEGSY VCKVIVDNKT YQGICFIGKP KTFDEKQRQC EAHIFDFDQD
IYGKKIKVEL YQFIRPTVKF NSINELKEAI ENDKKAALSF FHKQEKPKVV VALSGGVDSA
VCAYLLQQQG YDVVAAFMQN WDKDLNFELL SDHADDQIQG CDAKQDYEDT QKLCEQLKIK
LYHFNFVEQY WNDVFLKVLE DYKKGLTPNP DVLCNQFGKF GWFINALRKQ FGDDIKIAFG
HYAKLITKDD EVFLVHTKDH NKDQTYFLTM LKKEQLKNII FPLSELDKPT VREIAKQANL
YVANKKDSTG ICFIGERNFK QFLSNYLAIK KGPIILIDEN KKIGEHDGLY FYTIGQSRRL
HVGGTKEKIF VCDKDYNNNT LYVCYESSKD QYLSSVSCEL EKFNWLIDTK DQLFNKKLWI
RFRHRQKLQE CEIVSYHDDK VIVKYTKQIG VTPGQYGVIY DQNLWVVGGG KITKIIK
