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Q6ING7 (FLAD1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 57. 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length496 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

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
FAD
Flavoprotein
FMN
Nucleotide-binding
   Molecular functionNucleotidyltransferase
Transferase
Gene Ontology (GO)
   Biological_processFAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

Mo-molybdopterin cofactor biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

FMN adenylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496FAD synthase
PRO_0000302741

Regions

Region18 – 10992Molybdenum cofactor biosynthesis protein-like
Region307 – 464158FAD synthase

Sequences

Sequence LengthMass (Da)Tools
Q6ING7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D4252F3B84B672E3

FASTA49655,709
        10         20         30         40         50         60 
MTSTSPCLAT NVPPVTAGII IIGDEILKGH TQDTNSFFMC KKLRSIGVQV NKISVIPDDI 

        70         80         90        100        110        120 
DIIAGEIAGF SSRYTYVLTS GGIGPTHDDV TFEGVAKAFG EKTFPHPELV SLVQTFFGKS 

       130        140        150        160        170        180 
ESWCPEMKLA QIPVSSRLNY GTDKRTGDCF KYPLVSVGNV YVFPGIPSLL EKSLEGLDHL 

       190        200        210        220        230        240 
FRNDKTHFHY REICVSADEV AIAGVLGEVN GRFRKHVSLG SYPDWSNNYF RVLLVLDSHS 

       250        260        270        280        290        300 
EAHLEEAHKF LIEHLPPGVV VPFVKDPVTQ AAAQVYQLAH SGSPLGDKVA AALKTLEEAL 

       310        320        330        340        350        360 
DTYSLEKICV AFNGGKDCTA LLHLFHATVQ RKFPDQKDKL QALYIRIVSP FPEMEQFMQS 

       370        380        390        400        410        420 
TTKRYNLQIY TIQGYIKQAL VELKVEQPNL EAVLMGTRRS DPYSRTLTPM CLTDPDWPKY 

       430        440        450        460        470        480 
MRVNPLLDWS YRDIWDFLRT LFIPYCILYD KGYTSLGSME NTVKNPALRF TTPAGAESYH 

       490 
PAYKLQNEEE ERVSRK 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC072314 mRNA. Translation: AAH72314.1.
RefSeqNP_001085184.1. NM_001091715.1.
UniGeneXl.3706.

3D structure databases

ProteinModelPortalQ6ING7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID432268.
KEGGxla:432268.

Organism-specific databases

CTD80308.
XenbaseXB-GENE-5915969. flad1.

Phylogenomic databases

HOVERGENHBG058211.
KOK00953.

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. 1 hit.
[Graphical view]
PIRSFPIRSF036620. MPTbdFAD. 1 hit.
SMARTSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF53218. SSF53218. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFLAD1_XENLA
AccessionPrimary (citable) accession number: Q6ING7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: January 22, 2014
This is version 57 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