FMN adenylyltransferase
     (EC 2.7.7.2)
     (FAD pyrophosphorylase)
     (FAD synthetase)
Riboflavin kinase
     (EC 2.7.1.26)
     (Flavokinase)
tRNA-specific 2-thiouridylase mnmA
     (EC 2.8.1.-)

Gene name

	Name:	ribF/mnmA
	OrderedLocusNames:	MYCGA1200
	ORFNames:	MGA_0832

From

Mycoplasma gallisepticum

[TaxID: 2096]

[HAMAP proteome]

Taxonomy

Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=R(low);
DOI=10.1099/mic.0.26427-0; PubMed=12949158 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

FUNCTION: Involved in FAD and FMN biosynthesis (By similarity).
FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (By similarity).
CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN.
CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1 .
PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin: step 1/1 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the ribF family.
SIMILARITY: In the C-terminal section; belongs to the mnmA/TRMU family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE015450; AAP56470.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_852902.1; -.

3D structure databases

ModBase

Q7NBZ0.

Enzyme and pathway databases

BioCyc

MGAL233150:MGA_0832-MONOMER; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000049;	Molecular function: tRNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006400;	Biological process: tRNA modification (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00144; fused; 1.
PBIL [Tree]

InterPro

IPR015864; FAD_synthase.
IPR015865; Riboflavin_kinase.
IPR002606; Riboflavin_kinase/FAD_synth.
IPR004506; TrmU_MeTrfase.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.30.30; Riboflavin_kinase; 1.

PANTHER

PTHR11933; TrmU_mtfrase; 1.

Pfam

PF06574; FAD_syn; 1.
PF01687; Flavokinase; 1.
PF03054; tRNA_Me_trans; 1.
Pfam graphical view of domain structure.

ProDom

PD003662; FAD_Synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00083; ribF; 1.
TIGR00420; trmU; 1.

Genome annotation databases

GeneID

1090170; -.

GenomeReviews

AE015450_GR; MYCGA1200.

KEGG

mga:MGA_0832; -.

Phylogenomic databases

HOGENOM

Q7NBZ0; -.

Genome annotation databases

CMR

Q7NBZ0; MYCGA1200.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; FAD; FMN; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; RNA-binding; Transferase; tRNA processing; tRNA-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 657`	`657`	`Trifunctional protein ribF/mnmA.`	`PRO_0000349871`
`NP_BIND`	`292 299`	`8`	`ATP (By similarity).`
`REGION`	`1 141`	`141`	`FMN adenylyltransferase.`
`REGION`	`158 282`	`125`	`Riboflavin kinase.`
`REGION`	`283 657`	`375`	`tRNA-specific 2-thiouridylase mnmA.`
`REGION`	`389 391`	`3`	`Interaction with target base in tRNA (By similarity).`
`REGION`	`442 444`	`3`	`Interaction with tRNA (By similarity).`
`ACT_SITE`	`394 394`		`Nucleophile (By similarity).`
`ACT_SITE`	`492 492`		`Cysteine persulfide intermediate (By similarity).`
`BINDING`	`318 318`		`ATP; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`420 420`		`ATP; via amide nitrogen (By similarity).`
`SITE`	`421 421`	`1`	`Interaction with tRNA (By similarity).`
`SITE`	`635 635`	`1`	`Interaction with tRNA (By similarity).`
`DISULFID`	`394 492`		`Alternate (By similarity).`

Sequence information

Length: 657 AA [This is the length of the unprocessed precursor]

Molecular weight: 75974 Da [This is the MW of the unprocessed precursor]

CRC64: C2F795910B8821EF [This is a checksum on the sequence]

        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

Q7NBZ0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools