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Protein

FAD synthase

Gene

FAD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + FMN = diphosphate + FAD.

Pathway: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.
Proteins known to be involved in this subpathway in this organism are:
  1. FAD synthase (FAD1)
This subpathway is part of the pathway FAD biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FAD from FMN, the pathway FAD biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • FMN adenylyltransferase activity Source: SGD

GO - Biological processi

  • FAD biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YDL045C-MONOMER.
YEAST:YDL045C-MONOMER.
BRENDAi2.7.7.2. 984.
ReactomeiREACT_324957. Vitamin B2 (riboflavin) metabolism.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthase (EC:2.7.7.2)
Alternative name(s):
FAD pyrophosphorylase
FMN adenylyltransferase
Flavin adenine dinucleotide synthase
Gene namesi
Name:FAD1
Ordered Locus Names:YDL045C
ORF Names:D2702
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL045c.
EuPathDBiFungiDB:YDL045C.
SGDiS000002203. FAD1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306FAD synthasePRO_0000100691Add
BLAST

Proteomic databases

MaxQBiP38913.
PaxDbiP38913.

Interactioni

Protein-protein interaction databases

BioGridi32014. 10 interactions.
DIPiDIP-4735N.
IntActiP38913. 1 interaction.
MINTiMINT-515179.
STRINGi4932.YDL045C.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi25 – 4319Combined sources
Turni44 – 485Combined sources
Beta strandi51 – 599Combined sources
Helixi64 – 8724Combined sources
Beta strandi102 – 1065Combined sources
Helixi114 – 12613Combined sources
Beta strandi129 – 1335Combined sources
Helixi144 – 15411Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi189 – 1913Combined sources
Turni193 – 1964Combined sources
Helixi199 – 20911Combined sources
Helixi215 – 2184Combined sources
Turni227 – 2293Combined sources
Helixi234 – 2363Combined sources
Helixi238 – 2403Combined sources
Helixi248 – 2525Combined sources
Turni255 – 2573Combined sources
Helixi274 – 2796Combined sources
Turni280 – 2823Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 2983Combined sources
Turni299 – 3024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WSIX-ray1.90A1-306[»]
ProteinModelPortaliP38913.
SMRiP38913. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38913.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAPS reductase family. FAD1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0175.
GeneTreeiENSGT00390000007266.
HOGENOMiHOG000065966.
InParanoidiP38913.
KOiK00953.
OMAiWSFLLYS.
OrthoDBiEOG7DJSXH.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLSKAAEMC YEITNSYLHI DQKSQIIAST QEAIRLTRKY LLSEIFVRWS
60 70 80 90 100
PLNGEISFSY NGGKDCQVLL LLYLSCLWEY FFIKAQNSQF DFEFQSFPMQ
110 120 130 140 150
RLPTVFIDQE ETFPTLENFV LETSERYCLS LYESQRQSGA SVNMADAFRD
160 170 180 190 200
FIKIYPETEA IVIGIRHTDP FGEALKPIQR TDSNWPDFMR LQPLLHWDLT
210 220 230 240 250
NIWSFLLYSN EPICGLYGKG FTSIGGINNS LPNPHLRKDS NNPALHFEWE
260 270 280 290 300
IIHAFGKDAE GERSSAINTS PISVVDKERF SKYHDNYYPG WYLVDDTLER

AGRIKN
Length:306
Mass (Da):35,546
Last modified:February 1, 1995 - v1
Checksum:i55BBB830163A457F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12331 Genomic DNA. Translation: AAA65730.1.
Z71781 Genomic DNA. Translation: CAA96444.1.
Z74093 Genomic DNA. Translation: CAA98604.1.
AY558157 Genomic DNA. Translation: AAS56483.1.
BK006938 Genomic DNA. Translation: DAA11811.1.
PIRiS47906.
RefSeqiNP_010239.1. NM_001180104.1.

Genome annotation databases

EnsemblFungiiYDL045C; YDL045C; YDL045C.
GeneIDi851516.
KEGGisce:YDL045C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12331 Genomic DNA. Translation: AAA65730.1.
Z71781 Genomic DNA. Translation: CAA96444.1.
Z74093 Genomic DNA. Translation: CAA98604.1.
AY558157 Genomic DNA. Translation: AAS56483.1.
BK006938 Genomic DNA. Translation: DAA11811.1.
PIRiS47906.
RefSeqiNP_010239.1. NM_001180104.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WSIX-ray1.90A1-306[»]
ProteinModelPortaliP38913.
SMRiP38913. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32014. 10 interactions.
DIPiDIP-4735N.
IntActiP38913. 1 interaction.
MINTiMINT-515179.
STRINGi4932.YDL045C.

Proteomic databases

MaxQBiP38913.
PaxDbiP38913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL045C; YDL045C; YDL045C.
GeneIDi851516.
KEGGisce:YDL045C.

Organism-specific databases

CYGDiYDL045c.
EuPathDBiFungiDB:YDL045C.
SGDiS000002203. FAD1.

Phylogenomic databases

eggNOGiCOG0175.
GeneTreeiENSGT00390000007266.
HOGENOMiHOG000065966.
InParanoidiP38913.
KOiK00953.
OMAiWSFLLYS.
OrthoDBiEOG7DJSXH.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciMetaCyc:YDL045C-MONOMER.
YEAST:YDL045C-MONOMER.
BRENDAi2.7.7.2. 984.
ReactomeiREACT_324957. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

EvolutionaryTraceiP38913.
NextBioi968887.
PROiP38913.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae."
    Wu M., Repetto B., Glerum D.M., Tzagoloff A.
    Mol. Cell. Biol. 15:264-271(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: W303-1A / D273-10B.
  2. "The sequence of a 36.7 kb segment on the left arm of chromosome IV from Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1 and 11 new ORFs."
    Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.
    Yeast 13:65-71(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiFAD1_YEAST
AccessioniPrimary (citable) accession number: P38913
Secondary accession number(s): D6VRV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

FAD1 is essential for growth.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.