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Q7NBZ0 (MNMA_MYCGA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Trifunctional protein ribF/mnmA

Including the following 3 domains:

  1. FMN adenylyltransferase
    EC=2.7.7.2
    Alternative name(s):
    FAD pyrophosphorylase
    FAD synthase
  2. Riboflavin kinase
    EC=2.7.1.26
    Alternative name(s):
    Flavokinase
  3. tRNA-specific 2-thiouridylase mnmA
    EC=2.8.1.-
Gene names
Name:ribF/mnmA
Ordered Locus Names:MYCGA1200
ORF Names:MGA_0832
OrganismMycoplasma gallisepticum (strain R(low / passage 15 / clone 2)) [Complete proteome] [HAMAP]
Taxonomic identifier710127 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in FAD and FMN biosynthesis By similarity. HAMAP MF_00144

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s2U34 By similarity. HAMAP MF_00144

Catalytic activity

ATP + riboflavin = ADP + FMN. HAMAP MF_00144

ATP + FMN = diphosphate + FAD. HAMAP MF_00144

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. HAMAP MF_00144

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1. HAMAP MF_00144

Subcellular location

Cytoplasm By similarity HAMAP MF_00144.

Sequence similarities

In the N-terminal section; belongs to the ribF family.

In the C-terminal section; belongs to the mnmA/TRMU family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Trifunctional protein ribF/mnmA HAMAP MF_00144
PRO_0000349871

Regions

Nucleotide binding292 – 2998ATP By similarity
Region1 – 141141FMN adenylyltransferase HAMAP MF_00144
Region158 – 282125Riboflavin kinase HAMAP MF_00144
Region283 – 657375tRNA-specific 2-thiouridylase mnmA HAMAP MF_00144
Region389 – 3913Interaction with target base in tRNA By similarity
Region442 – 4443Interaction with tRNA By similarity

Sites

Active site3941Nucleophile By similarity
Active site4921Cysteine persulfide intermediate By similarity
Binding site3181ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site4201ATP; via amide nitrogen By similarity
Site4211Interaction with tRNA By similarity
Site6351Interaction with tRNA By similarity

Amino acid modifications

Disulfide bond394 ↔ 492Alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NBZ0 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: C2F795910B8821EF

FASTA65775,974
        10         20         30         40         50         60 
MLSIINLTSK TIKEVNKGVD LVIGFFDGIH KGHAKLFKQS DRFNLLTFDH IPKKQRLLYP 

        70         80         90        100        110        120 
KVDEIEQLSA LSGLEQLLVY DLLNNNLSAQ EFIDNYIKLI QPKRIIVGSD FKFGSDQVDY 

       130        140        150        160        170        180 
SLFAKNGYEV VVVKKDHCST SEIKKLIINC DLDQANKLLL TPFYLKGTVI KNAQRGRTIG 

       190        200        210        220        230        240 
FVTANIILDN QLIELTEGSY VCKVIVDNKT YQGICFIGKP KTFDEKQRQC EAHIFDFDQD 

       250        260        270        280        290        300 
IYGKKIKVEL YQFIRPTVKF NSINELKEAI ENDKKAALSF FHKQEKPKVV VALSGGVDSA 

       310        320        330        340        350        360 
VCAYLLQQQG YDVVAAFMQN WDKDLNFELL SDHADDQIQG CDAKQDYEDT QKLCEQLKIK 

       370        380        390        400        410        420 
LYHFNFVEQY WNDVFLKVLE DYKKGLTPNP DVLCNQFGKF GWFINALRKQ FGDDIKIAFG 

       430        440        450        460        470        480 
HYAKLITKDD EVFLVHTKDH NKDQTYFLTM LKKEQLKNII FPLSELDKPT VREIAKQANL 

       490        500        510        520        530        540 
YVANKKDSTG ICFIGERNFK QFLSNYLAIK KGPIILIDEN KKIGEHDGLY FYTIGQSRRL 

       550        560        570        580        590        600 
HVGGTKEKIF VCDKDYNNNT LYVCYESSKD QYLSSVSCEL EKFNWLIDTK DQLFNKKLWI 

       610        620        630        640        650 
RFRHRQKLQE CEIVSYHDDK VIVKYTKQIG VTPGQYGVIY DQNLWVVGGG KITKIIK

« Hide

References

[1]"The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low)."
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.
Microbiology 149:2307-2316(2003) [PubMed: 12949158] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R(low / passage 15 / clone 2).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015450 Genomic DNA. Translation: AAP56470.1.
RefSeqNP_852902.1. NC_004829.2.

3D structure databases

ProteinModelPortalQ7NBZ0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1090170.
GenomeReviewsGene locus MYCGA1200 in contig AE015450_GR.
KEGGmga:MGA_0832.
PATRIC20007937. VBIMycGal115357_0134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

PhylomeDBQ7NBZ0.

Family and domain databases

HAMAPMF_00144. tRNA_thiouridyl_MnmA. Fused.
[Tree]
InterProIPR023382. Adenine_a_hdrlase_dom.
IPR015864. FAD_synthase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
Gene3DG3DSA:2.30.30.280. G3DSA:2.30.30.280. 1 hit.
G3DSA:2.40.30.30. Riboflavin_kinase. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
PANTHERPTHR11933. TrmU_mtfrase. 1 hit.
PfamPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
PF03054. tRNA_Me_trans. 1 hit.
[Graphical view]
SMARTSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMSSF82114. Riboflavin_kinase. 1 hit.
TIGRFAMsTIGR00083. RibF. 1 hit.
TIGR00420. TrmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNMA_MYCGA
AccessionPrimary (citable) accession number: Q7NBZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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