ENZYME entry: EC 2.7.7.2

Accepted Name

FAD synthase

Alternative Name(s)

FAD diphosphorylase

FAD pyrophosphorylase

FADS

flavin adenine dinucleotide synthetase

FMN adenylyltransferase

Reaction catalysed

ATP + FMN + H(+) <=> diphosphate + FAD

Comment(s)

Highly specific for ATP as phosphate donor.
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.

Cross-references

BRENDA

2.7.7.2

EC2PDB

2.7.7.2

ExplorEnz

2.7.7.2

PRIAM enzyme-specific profiles

2.7.7.2

KEGG Ligand Database for Enzyme Nomenclature

2.7.7.2

IUBMB Enzyme Nomenclature

2.7.7.2

IntEnz

2.7.7.2

MEDLINE

Find literature relating to 2.7.7.2

MetaCyc

2.7.7.2

Rhea expert-curated reactions

2.7.7.2

UniProtKB/Swiss-Prot

Q626I0, FAD1_CAEBR	Q22017, FAD1_CAEEL	Q68EH8, FAD1_DANRE
Q8NFF5, FAD1_HUMAN	Q8R123, FAD1_MOUSE	Q5RCH4, FAD1_PONAB
O74841, FAD1_SCHPO	P38913, FAD1_YEAST	Q6ING7, FLAD1_XENLA
Q7NBZ0, MNMA_MYCGA	Q8Y7F2, RIBCF_LISMO	P54575, RIBC_BACSU
Q8Y914, RIBC_LISMO	Q9FMW8, RIBF1_ARATH	Q8VZR0, RIBF2_ARATH
P57250, RIBF_BUCAI	Q8K9Z1, RIBF_BUCAP	Q59263, RIBF_CORAM
P0AG42, RIBF_ECO57	P0AG41, RIBF_ECOL6	P0AG40, RIBF_ECOLI
A4IT50, RIBF_GEOTN	P44957, RIBF_HAEIN	P47391, RIBF_MYCGE
P75587, RIBF_MYCPN	Q10BX9, RIBF_ORYSJ	P22990, RIBF_PSEFL
O84990, RIBF_RHOOP	P0AG43, RIBF_SHIFL	P73651, RIBF_SYNY3
B5I9H4, RIBL_ACIB4	O28854, RIBL_ARCFU	D2RES5, RIBL_ARCPA
D3RZA9, RIBL_FERPA	D8J4S4, RIBL_HALJB	B9LSN4, RIBL_HALLT
C7P4K0, RIBL_HALMD	B0R450, RIBL_HALS3	Q9HRB2, RIBL_HALSA
D2RTP8, RIBL_HALTV	C7NTR1, RIBL_HALUD	D4GVJ2, RIBL_HALVD
B1L7J8, RIBL_KORCO	A6UWK8, RIBL_META3	Q8TPT5, RIBL_METAC
Q0W933, RIBL_METAR	A7I4S0, RIBL_METB6	Q46AS7, RIBL_METBF
Q12YR1, RIBL_METBU	D7E8Z9, RIBL_METEZ	C7P607, RIBL_METFA
E3GWN9, RIBL_METFV	Q2FT79, RIBL_METHJ	D5VUB0, RIBL_METIM
Q58579, RIBL_METJA	Q8TXT2, RIBL_METKA	A2SQH8, RIBL_METLZ
A4FXX6, RIBL_METM5	A9AB01, RIBL_METM6	A6VFN4, RIBL_METM7
Q8Q095, RIBL_METMA	A3CXW9, RIBL_METMJ	Q6LYP5, RIBL_METMP
D5EBS7, RIBL_METMS	E1RHM5, RIBL_METP4	B8GJN8, RIBL_METPE
D1YZF2, RIBL_METPS	D3DZ18, RIBL_METRM	A5ULI6, RIBL_METS3
D3S3T0, RIBL_METSF	Q2NHB2, RIBL_METST	O26932, RIBL_METTH
D9PX81, RIBL_METTM	A0B7A6, RIBL_METTP	D7DTT8, RIBL_METV3
C9RF94, RIBL_METVM	A6UNT3, RIBL_METVS	D3SYU6, RIBL_NATMM
Q3IQ95, RIBL_NATPD	Q6L0A7, RIBL_PICTO	Q9UZ37, RIBL_PYRAB
Q8U1T9, RIBL_PYRFU	O58466, RIBL_PYRHO	Q9HJ34, RIBL_THEAC
C5A1S7, RIBL_THEGJ	Q5JHT4, RIBL_THEKO	B6YXC8, RIBL_THEON
C6A439, RIBL_THESM	Q979C2, RIBL_THEVO

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.

All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.7.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-