Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5RCH4 (FAD1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD synthase

EC=2.7.7.2
Alternative name(s):
FAD pyrophosphorylase
FMN adenylyltransferase
Flavin adenine dinucleotide synthase

Including the following 2 domains:

  1. Molybdenum cofactor biosynthesis protein-like region
  2. FAD synthase region
Gene names
Name:FLAD1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme By similarity.

Catalytic activity

ATP + FMN = diphosphate + FAD.

Cofactor

Magnesium By similarity.

Pathway

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

Subcellular location

Cytoplasm By similarity.

Domain

The molybdenum cofactor biosynthesis protein-like region may not be functional.

Sequence similarities

In the N-terminal section; belongs to the MoaB/Mog family.

In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491FAD synthase
PRO_0000302739

Regions

Region17 – 10892Molybdenum cofactor biosynthesis protein-like
Region302 – 459158FAD synthase

Amino acid modifications

Modified residue91Phosphoserine By similarity
Modified residue2821N6-acetyllysine; alternate By similarity
Modified residue2821N6-succinyllysine; alternate By similarity
Modified residue4671Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCH4 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: BD18AD9F84592F52

FASTA49154,307
        10         20         30         40         50         60 
MTSRASELSP GRSVTAGIII VGDEILKGHT QDTNTFFLCR TLRSLGVQVC RVSVAPDEVA 

        70         80         90        100        110        120 
TIAAEVTSFS NRFTHVLTAG GIGPTHDDVT FEAVAQAFGD ELKPHPELEA ATKALGGEGW 

       130        140        150        160        170        180 
EKLSLVPSSA CLHYGTDPRT GHPFRFPLVS VRNVYLFPSI PELLRRVLEG MKGLFQNPAV 

       190        200        210        220        230        240 
QFHSKELYVA ADEASIAPIL AEAQAHFGRR LGLGSYPDWG SNYYQVKLTL DSRGRRIPGG 

       250        260        270        280        290        300 
NAWPNLTARL PQGSLVPYMP NAVEQASEAV YKLAESGSSL GKKVAGALQT IETALAQYSL 

       310        320        330        340        350        360 
TQLCVGFNGG KDCTALLHLF HAAVQRKLPD VPNPLQILYI RSISPFPELE QFLQDTIKRY 

       370        380        390        400        410        420 
NLQMLEAEGS MKQALGELQA RHPQLEAVLM GTRRTDPYSC SLCPFSPTDP GWPAFMRINP 

       430        440        450        460        470        480 
LLDWTYRDIW DFLRQLFVPY CILYDRGYTS LGSRENTVRD PALKRLSPGG HPTYRPAYLL 

       490 
ENEEEERNSR T 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858296 mRNA. Translation: CAH90533.1.
UniGenePab.13439.

3D structure databases

ProteinModelPortalQ5RCH4.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RCH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG058211.

Enzyme and pathway databases

UniPathwayUPA00277; UER00407.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProIPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 2 hits.
[Graphical view]
PIRSFPIRSF036620. MPTbdFAD. 1 hit.
SMARTSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF53218. SSF53218. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFAD1_PONAB
AccessionPrimary (citable) accession number: Q5RCH4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways