Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.2 - FAD synthase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC2.7.7.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.2 FAD synthase
IUBMB Comments
Requires Mg2+ and is 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, riboflavin kinase [3,5].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
fads1, flad1, fad synthase, fad pyrophosphorylase, flavin adenine dinucleotide synthetase, atp:fmn adenylyltransferase, atribf1, atribf2, mj1179, fmn:atp adenylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine triphosphate-riboflavin mononucleotide transadenylase
-
-
-
-
adenosine triphosphate-riboflavine mononucleotide transadenylase
-
-
-
-
FAD pyrophosphorylase
-
-
-
-
FMN adenylyltransferase
-
-
-
-
FMN pyrophosphorylase
-
-
-
-
lysZ
-
-
-
-
riboflavin adenine dinucleotide pyrophosphorylase
-
-
-
-
riboflavin mononucleotide adenylyltransferase
-
-
-
-
riboflavine adenine dinucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:FMN adenylyltransferase
Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. 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 [3]. 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, riboflavin kinase [3,5].
CAS REGISTRY NUMBER
COMMENTARY hide
9026-37-3
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0C6F617_PSEAI
312
0
34310
TrEMBL
-
A0A8B4ZF46_PSEAI
312
0
34370
TrEMBL
-
A0A8G5ITB3_PSEAI
312
0
34410
TrEMBL
-
A0A643J720_PSEAI
312
0
34368
TrEMBL
-
A0A485G8C3_PSEAI
244
0
27013
TrEMBL
-
A0A0F7QXG9_PSEAI
312
0
34340
TrEMBL
-
A0A8F9P7S0_PSEAI
312
0
34276
TrEMBL
-
A0A8G2VT83_PSEAI
312
0
34368
TrEMBL
-
A0A8G7SDJ7_PSEAI
312
0
34313
TrEMBL
-
A0A8G2UWW2_PSEAI
312
0
34358
TrEMBL
-
A0A2R3J1J4_PSEAI
312
0
34327
TrEMBL
-
A0A0A8RKR1_PSEAI
312
0
34281
TrEMBL
-
A0A8G1NK64_PSEAI
312
0
34398
TrEMBL
-
A0A5K1SES1_PSEAI
312
0
34312
TrEMBL
-
A0A8G3ZPJ3_PSEAI
312
0
34250
TrEMBL
-
A0A8F9KIP5_PSEAI
312
0
34326
TrEMBL
-