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Trifunctional protein RibF/MnmA [Includes: FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthase); Riboflavin kinase (EC 2.7.1.26) (Flavokinase); tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13)]

 MNMA_MYCGA              Reviewed;         657 AA.
Q7NBZ0;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
07-JUN-2017, entry version 88.
RecName: Full=Trifunctional protein RibF/MnmA;
Includes:
RecName: Full=FMN adenylyltransferase;
EC=2.7.7.2;
AltName: Full=FAD pyrophosphorylase;
AltName: Full=FAD synthase;
Includes:
RecName: Full=Riboflavin kinase;
EC=2.7.1.26;
AltName: Full=Flavokinase;
Includes:
RecName: Full=tRNA-specific 2-thiouridylase MnmA;
EC=2.8.1.13;
Name=ribF/mnmA; OrderedLocusNames=MYCGA1200; ORFNames=MGA_0832;
Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2)).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=710127;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=R(low / passage 15 / clone 2);
PubMed=12949158; DOI=10.1099/mic.0.26427-0;
Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
"The complete genome sequence of the avian pathogen Mycoplasma
gallisepticum strain R(low).";
Microbiology 149:2307-2316(2003).
-!- FUNCTION: Involved in FAD and FMN biosynthesis. {ECO:0000250}.
-!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble
position (U34) of tRNA, leading to the formation of s(2)U34.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN.
-!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
-!- CATALYTIC ACTIVITY: A [protein]-S-sulfanyl-L-cysteine +
uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-
cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate +
acceptor.
-!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN:
step 1/1.
-!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from
riboflavin (ATP route): step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the RibF family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the MnmA/TRMU
family. {ECO:0000305}.
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EMBL; AE015450; AAP56470.1; -; Genomic_DNA.
RefSeq; WP_011113349.1; NC_004829.2.
ProteinModelPortal; Q7NBZ0; -.
SMR; Q7NBZ0; -.
PRIDE; Q7NBZ0; -.
EnsemblBacteria; AAP56470; AAP56470; MGA_0832.
GeneID; 1090170; -.
KEGG; mga:MGA_0832; -.
PATRIC; fig|233150.7.peg.134; -.
HOGENOM; HOG000113614; -.
OMA; VSCELEN; -.
BioCyc; MGAL710127:GC09-124-MONOMER; -.
UniPathway; UPA00276; UER00406.
UniPathway; UPA00277; UER00407.
Proteomes; UP000001418; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
CDD; cd01998; tRNA_Me_trans; 1.
Gene3D; 2.30.30.280; -; 1.
Gene3D; 2.40.30.30; -; 1.
Gene3D; 3.40.50.620; -; 2.
HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
InterPro; IPR023382; Adenine_a_hdrlase_dom.
InterPro; IPR015864; FAD_synthase.
InterPro; IPR002606; Riboflavin_kinase_bac.
InterPro; IPR015865; Riboflavin_kinase_bac/euk.
InterPro; IPR023465; Riboflavin_kinase_domain.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR004506; tRNA-specific_2-thiouridylase.
PANTHER; PTHR11933; PTHR11933; 1.
Pfam; PF06574; FAD_syn; 1.
Pfam; PF01687; Flavokinase; 1.
SMART; SM00904; Flavokinase; 1.
SUPFAM; SSF82114; SSF82114; 1.
TIGRFAMs; TIGR00083; ribF; 1.
TIGRFAMs; TIGR00420; trmU; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; FAD;
Flavoprotein; FMN; Kinase; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase;
tRNA processing; tRNA-binding.
CHAIN 1 657 Trifunctional protein RibF/MnmA.
/FTId=PRO_0000349871.
NP_BIND 292 299 ATP. {ECO:0000250}.
REGION 1 141 FMN adenylyltransferase.
REGION 158 282 Riboflavin kinase.
REGION 283 657 tRNA-specific 2-thiouridylase MnmA.
REGION 389 391 Interaction with target base in tRNA.
{ECO:0000250}.
REGION 442 444 Interaction with tRNA. {ECO:0000250}.
ACT_SITE 394 394 Nucleophile. {ECO:0000250}.
ACT_SITE 492 492 Cysteine persulfide intermediate.
{ECO:0000250}.
BINDING 318 318 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 420 420 ATP; via amide nitrogen. {ECO:0000250}.
SITE 421 421 Interaction with tRNA. {ECO:0000250}.
SITE 635 635 Interaction with tRNA. {ECO:0000250}.
DISULFID 394 492 Alternate. {ECO:0000250}.
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


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