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Q8NFF5 (FAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
ORF Names:PP591
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + FMN = diphosphate + FAD. Ref.1

Cofactor

Magnesium. Ref.1 Ref.9

Pathway

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

Subcellular location

Isoform 1: Mitochondrion matrix Ref.13.

Isoform 2: Cytoplasm Ref.13.

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.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 µM for FMN (Ref.1) Ref.1 Ref.9

KM=0.36 µM for FMN (isoform 2)(Ref.9)

Vmax=6.1 nmol/min/mg enzyme (Ref.1)

Vmax=3.9 nmol/min/mg enzyme (isoform 2)(Ref.9)

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NFF5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8NFF5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
Isoform 3 (identifier: Q8NFF5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
     544-587: Missing.
Isoform 4 (identifier: Q8NFF5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
     374-393: SSLGKKVAGALQTIETSLAQ → RDLMEEGHYAQSHWWHPRSQ
     394-587: Missing.
Isoform 5 (identifier: Q8NFF5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
     374-437: SSLGKKVAGA...PNPLQILYIR → NYLMFQTPSR...WMGPFPGQQG
     438-587: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1717Mitochondrion Potential
Chain18 – 587570FAD synthase
PRO_0000302737

Regions

Region114 – 20592Molybdenum cofactor biosynthesis protein-like
Region398 – 555158FAD synthase

Amino acid modifications

Modified residue1061Phosphoserine Ref.10 Ref.11
Modified residue3781N6-acetyllysine; alternate By similarity
Modified residue3781N6-succinyllysine; alternate By similarity
Modified residue5631Phosphoserine Ref.10 Ref.12

Natural variations

Alternative sequence1 – 9797Missing in isoform 2 and isoform 3.
VSP_027947
Alternative sequence1 – 3030Missing in isoform 4 and isoform 5.
VSP_027948
Alternative sequence31 – 12494LEGST…DEILK → MQPSSSTPPLHPYSTDGLIF PFNPQ in isoform 4 and isoform 5.
VSP_027949
Alternative sequence374 – 43764SSLGK…ILYIR → NYLMFQTPSRSCISAASPLS LSWNSFYRTLSREQAIPENQ IASPPSEAKGAEEPWMGPFP GQQG in isoform 5.
VSP_027950
Alternative sequence374 – 39320SSLGK…TSLAQ → RDLMEEGHYAQSHWWHPRSQ in isoform 4.
VSP_027951
Alternative sequence394 – 587194Missing in isoform 4.
VSP_027952
Alternative sequence438 – 587150Missing in isoform 5.
VSP_027953
Alternative sequence544 – 58744Missing in isoform 3.
VSP_027954

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F95918B15D9D8106

FASTA58765,266
        10         20         30         40         50         60 
MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG 

        70         80         90        100        110        120 
YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD 

       130        140        150        160        170        180 
EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG 

       190        200        210        220        230        240 
PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP 

       250        260        270        280        290        300 
FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA 

       310        320        330        340        350        360 
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE 

       370        380        390        400        410        420 
QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV 

       430        440        450        460        470        480 
QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ 

       490        500        510        520        530        540 
LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY 

       550        560        570        580 
DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT 

« Hide

Isoform 2 [UniParc].

Checksum: 633D7949AB88E059
Show »

FASTA49054,188
Isoform 3 [UniParc].

Checksum: 2983E4FA84020CDF
Show »

FASTA44649,198
Isoform 4 [UniParc].

Checksum: 5CEF3426F7FEDEF5
Show »

FASTA29432,369
Isoform 5 [UniParc].

Checksum: 2BB52386763E2A9B
Show »

FASTA33836,865

References

« Hide 'large scale' references
[1]"Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase."
Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V., Accardi R., Gianazza E., Indiveri C., Barile M.
Biochem. Biophys. Res. Commun. 344:1008-1016(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
Tissue: Skin.
[2]"Cloning, expression and characterization of a human FAD synthetase."
Fischer M.J., Kempter K., Bacher A.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[3]Chen X.G., Li Y.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Skin.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1).
Tissue: Brain, Colon, Placenta and Skin.
[8]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1).
Tissue: Brain.
[9]"Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase."
Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E., Indiveri C., Barile M.
Protein Expr. Purif. 52:175-181(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Mitochondrial localization of human FAD synthetase isoform 1."
Torchetti E.M., Brizio C., Colella M., Galluccio M., Giancaspero T.A., Indiveri C., Roberti M., Barile M.
Mitochondrion 10:263-273(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ458779 mRNA. Translation: ABE65383.1.
AF481877 mRNA. Translation: AAO49318.1.
AF520568 mRNA. Translation: AAM77338.1.
AF218022 mRNA. Translation: AAG17264.1.
AL451085 Genomic DNA. Translation: CAI13259.1.
AL451085 Genomic DNA. Translation: CAI13260.1.
AL451085 Genomic DNA. Translation: CAI13261.1.
AL451085 Genomic DNA. Translation: CAI13262.1.
CH471121 Genomic DNA. Translation: EAW53154.1.
CH471121 Genomic DNA. Translation: EAW53155.1.
CH471121 Genomic DNA. Translation: EAW53158.1.
CH471121 Genomic DNA. Translation: EAW53159.1.
BC011378 mRNA. Translation: AAH11378.1.
BC014012 mRNA. Translation: AAH14012.2.
BC020253 mRNA. Translation: AAH20253.1.
BC021096 mRNA. Translation: AAH21096.2.
BC032323 mRNA. Translation: AAH32323.1.
U79241 mRNA. Translation: AAB50199.1.
CCDSCCDS1078.1. [Q8NFF5-1]
CCDS1079.1. [Q8NFF5-2]
CCDS53371.1. [Q8NFF5-3]
CCDS53372.1. [Q8NFF5-4]
RefSeqNP_001171820.1. NM_001184891.1. [Q8NFF5-3]
NP_001171821.1. NM_001184892.1. [Q8NFF5-4]
NP_079483.3. NM_025207.4. [Q8NFF5-1]
NP_958800.1. NM_201398.2. [Q8NFF5-2]
UniGeneHs.118666.

3D structure databases

ProteinModelPortalQ8NFF5.
SMRQ8NFF5. Positions 113-269, 349-560.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123221. 16 interactions.
IntActQ8NFF5. 13 interactions.
MINTMINT-3042841.
STRING9606.ENSP00000292180.

PTM databases

PhosphoSiteQ8NFF5.

Polymorphism databases

DMDM74751275.

Proteomic databases

MaxQBQ8NFF5.
PaxDbQ8NFF5.
PRIDEQ8NFF5.

Protocols and materials databases

DNASU80308.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292180; ENSP00000292180; ENSG00000160688. [Q8NFF5-1]
ENST00000315144; ENSP00000317296; ENSG00000160688. [Q8NFF5-2]
ENST00000368431; ENSP00000357416; ENSG00000160688. [Q8NFF5-4]
ENST00000368432; ENSP00000357417; ENSG00000160688. [Q8NFF5-3]
ENST00000405236; ENSP00000384323; ENSG00000160688. [Q8NFF5-5]
GeneID80308.
KEGGhsa:80308.
UCSCuc001fgc.3. human. [Q8NFF5-4]
uc001fgd.2. human. [Q8NFF5-1]

Organism-specific databases

CTD80308.
GeneCardsGC01P154955.
HGNCHGNC:24671. FLAD1.
HPAHPA028476.
HPA028486.
HPA028563.
MIM610595. gene.
neXtProtNX_Q8NFF5.
PharmGKBPA142671759.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0175.
HOVERGENHBG058211.
InParanoidQ8NFF5.
KOK00953.
OMAAIAVEIS.
OrthoDBEOG7C5M9F.
PhylomeDBQ8NFF5.
TreeFamTF314056.

Enzyme and pathway databases

BioCycMetaCyc:HS08520-MONOMER.
BRENDA2.7.7.2. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ8NFF5.
UniPathwayUPA00277; UER00407.

Gene expression databases

ArrayExpressQ8NFF5.
BgeeQ8NFF5.
CleanExHS_FLAD1.
GenevestigatorQ8NFF5.

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...

Other

ChiTaRSFLAD1. human.
GenomeRNAi80308.
NextBio70783.
PROQ8NFF5.
SOURCESearch...

Entry information

Entry nameFAD1_HUMAN
AccessionPrimary (citable) accession number: Q8NFF5
Secondary accession number(s): Q8N5J1 expand/collapse secondary AC list , Q8N686, Q8WU93, Q8WUJ4, Q96CR8, Q99764, Q9HBN6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM