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P38913

- FAD1_YEAST

UniProt

P38913 - FAD1_YEAST

Protein

FAD synthase

Gene

FAD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    ATP + FMN = diphosphate + FAD.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FMN adenylyltransferase activity Source: SGD

    GO - Biological processi

    1. FAD biosynthetic process Source: SGD

    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.
    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: Chromosome IV

    Organism-specific databases

    CYGDiYDL045c.
    SGDiS000002203. FAD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    MaxQBiP38913.
    PaxDbiP38913.

    Expressioni

    Gene expression databases

    GenevestigatoriP38913.

    Interactioni

    Protein-protein interaction databases

    BioGridi32014. 9 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 – 1816
    Helixi25 – 4319
    Turni44 – 485
    Beta strandi51 – 599
    Helixi64 – 8724
    Beta strandi102 – 1065
    Helixi114 – 12613
    Beta strandi129 – 1335
    Helixi144 – 15411
    Beta strandi160 – 1623
    Beta strandi169 – 1713
    Beta strandi177 – 1804
    Beta strandi189 – 1913
    Turni193 – 1964
    Helixi199 – 20911
    Helixi215 – 2184
    Turni227 – 2293
    Helixi234 – 2363
    Helixi238 – 2403
    Helixi248 – 2525
    Turni255 – 2573
    Helixi274 – 2796
    Turni280 – 2823
    Helixi290 – 2923
    Helixi296 – 2983
    Turni299 – 3024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MQLSKAAEMC YEITNSYLHI DQKSQIIAST QEAIRLTRKY LLSEIFVRWS    50
    PLNGEISFSY NGGKDCQVLL LLYLSCLWEY FFIKAQNSQF DFEFQSFPMQ 100
    RLPTVFIDQE ETFPTLENFV LETSERYCLS LYESQRQSGA SVNMADAFRD 150
    FIKIYPETEA IVIGIRHTDP FGEALKPIQR TDSNWPDFMR LQPLLHWDLT 200
    NIWSFLLYSN EPICGLYGKG FTSIGGINNS LPNPHLRKDS NNPALHFEWE 250
    IIHAFGKDAE GERSSAINTS PISVVDKERF SKYHDNYYPG WYLVDDTLER 300
    AGRIKN 306
    Length:306
    Mass (Da):35,546
    Last modified:February 1, 1995 - v1
    Checksum:i55BBB830163A457F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S47906.
    RefSeqi NP_010239.1. NM_001180104.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WSI X-ray 1.90 A 1-306 [» ]
    ProteinModelPortali P38913.
    SMRi P38913. Positions 1-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32014. 9 interactions.
    DIPi DIP-4735N.
    IntActi P38913. 1 interaction.
    MINTi MINT-515179.
    STRINGi 4932.YDL045C.

    Proteomic databases

    MaxQBi P38913.
    PaxDbi P38913.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL045C ; YDL045C ; YDL045C .
    GeneIDi 851516.
    KEGGi sce:YDL045C.

    Organism-specific databases

    CYGDi YDL045c.
    SGDi S000002203. FAD1.

    Phylogenomic databases

    eggNOGi COG0175.
    GeneTreei ENSGT00390000007266.
    HOGENOMi HOG000065966.
    KOi K00953.
    OMAi WSFLLYS.
    OrthoDBi EOG7DJSXH.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci MetaCyc:YDL045C-MONOMER.
    YEAST:YDL045C-MONOMER.
    BRENDAi 2.7.7.2. 984.

    Miscellaneous databases

    EvolutionaryTracei P38913.
    NextBioi 968887.
    PROi P38913.

    Gene expression databases

    Genevestigatori P38913.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR002500. PAPS_reduct.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF01507. PAPS_reduct. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 110 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