Reviewed,
UniProtKB/Swiss-Prot Q7NBZ0 (MNMA_MYCGA)
Last modified
June 16, 2009.
Version 34.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Trifunctional protein ribF/mnmA Including the following 3 domains: 1- Recommended name: FMN adenylyltransferase EC=2.7.7.2 Alternative name(s): FAD pyrophosphorylase FAD synthetase 2- Recommended name: Riboflavin kinase EC=2.7.1.26 Alternative name(s): Flavokinase 3- Recommended name: tRNA-specific 2-thiouridylase mnmA EC=2.8.1.- | ||||||
| Gene names |
| ||||||
| Organism | Mycoplasma gallisepticum [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 2096 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma |
Protein attributes
| Sequence length | 657 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in FAD and FMN biosynthesis By similarity. Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s2U34 By similarity. |
| 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. |
| Sequence similarities | In the N-terminal section; belongs to the ribF family. In the C-terminal section; belongs to the mnmA/TRMU family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding FAD FMN Nucleotide-binding RNA-binding tRNA-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| PTM | Disulfide bond |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | riboflavin biosynthetic process Inferred from electronic annotation. Source: InterPro tRNA modificationInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FMN adenylyltransferase activityInferred from electronic annotation. Source: EC riboflavin kinase activityInferred from electronic annotation. Source: EC tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activityInferred from electronic annotation. Source: InterPro tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 657 | 657 | Trifunctional protein ribF/mnmA HAMAP MF_00144 | PRO_0000349871 | |||||||
Regions | |||||||||||
| Nucleotide binding | 292 – 299 | 8 | ATP By similarity | ||||||||
| Region | 1 – 141 | 141 | FMN adenylyltransferase HAMAP MF_00144 | ||||||||
| Region | 158 – 282 | 125 | Riboflavin kinase HAMAP MF_00144 | ||||||||
| Region | 283 – 657 | 375 | tRNA-specific 2-thiouridylase mnmA HAMAP MF_00144 | ||||||||
| Region | 389 – 391 | 3 | Interaction with target base in tRNA By similarity | ||||||||
| Region | 442 – 444 | 3 | Interaction with tRNA By similarity | ||||||||
Sites | |||||||||||
| Active site | 394 | 1 | Nucleophile By similarity | ||||||||
| Active site | 492 | 1 | Cysteine persulfide intermediate By similarity | ||||||||
| Binding site | 318 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 420 | 1 | ATP; via amide nitrogen By similarity | ||||||||
| Site | 421 | 1 | Interaction with tRNA By similarity | ||||||||
| Site | 635 | 1 | Interaction with tRNA By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 394 ↔ 492 | Alternate By similarity | |||||||||
Sequences
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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). |
Cross-references
Sequence databases | |
|---|---|
| AE015450 Genomic DNA. Translation: AAP56470.1. | |
| RefSeq | NP_852902.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1090170. |
| GenomeReviews | Gene locus MYCGA1200 in contig AE015450_GR. |
| KEGG | mga:MGA_0832. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7NBZ0. |
Enzyme and pathway databases | |
| BioCyc | MGAL233150:MGA_0832-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00144. Fused. [Tree] |
| InterPro | IPR015864. FAD_synthase. IPR015865. Riboflavin_kinase. IPR002606. Riboflavin_kinase/FAD_synth. IPR004506. TrmU_MeTrfase. IPR018318. tRNA_MeTrfase-like. [Graphical view] |
| Gene3D | G3DSA:2.40.30.30. Riboflavin_kinase. 1 hit. |
| PANTHER | PTHR11933. TrmU_mtfrase. 1 hit. |
| Pfam | PF06574. FAD_syn. 1 hit. PF01687. Flavokinase. 1 hit. PF03054. tRNA_Me_trans. 1 hit. [Graphical view] |
| ProDom | PD003662. FAD_Synth. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00083. ribF. 1 hit. TIGR00420. trmU. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MNMA_MYCGA | ||||||||
| Accession | Primary (citable) accession number: Q7NBZ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


