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   27-MAR-2024, entry version 114.
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   Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasma gallisepticum).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
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   MoonProt; Q7NBZ0; -.
DR   KEGG; mga:MGA_0832; -.
DR   PATRIC; fig|233150.7.peg.134; -.
DR   HOGENOM; CLU_417276_0_0_14; -.
DR   OrthoDB; 9800696at2; -.
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; Adenine nucleotide alpha hydrolases-like domains; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR015864; FAD_synthase.
DR   InterPro; IPR046885; MnmA-like_C.
DR   InterPro; IPR046884; MnmA-like_central.
DR   InterPro; IPR023382; MnmA-like_central_sf.
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   NCBIfam; TIGR00083; ribF; 1.
DR   NCBIfam; TIGR00420; trmU; 1.
DR   PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR   PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR   Pfam; PF06574; FAD_syn; 1.
DR   Pfam; PF01687; Flavokinase; 1.
DR   Pfam; PF03054; tRNA_Me_trans; 1.
DR   Pfam; PF20258; tRNA_Me_trans_C; 1.
DR   Pfam; PF20259; tRNA_Me_trans_M; 1.
DR   SMART; SM00904; Flavokinase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF82114; Riboflavin kinase-like; 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
//