FAD1_YEAST
ID FAD1_YEAST Reviewed; 306 AA.
AC P38913; D6VRV1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Flavin adenine dinucleotide synthase {ECO:0000303|PubMed:7799934};
DE Short=FAD synthase {ECO:0000303|PubMed:7799934};
DE EC=2.7.7.2 {ECO:0000269|PubMed:7799934};
DE AltName: Full=FAD pyrophosphorylase;
DE AltName: Full=FMN adenylyltransferase;
GN Name=FAD1 {ECO:0000303|PubMed:7799934}; OrderedLocusNames=YDL045C;
GN ORFNames=D2702;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=W303-1A / D273-10B;
RX PubMed=7799934; DOI=10.1128/mcb.15.1.264;
RA Wu M., Repetto B., Glerum D.M., Tzagoloff A.;
RT "Cloning and characterization of FAD1, the structural gene for flavin
RT adenine dinucleotide synthetase of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:264-271(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046088;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT "The sequence of a 36.7 kb segment on the left arm of chromosome IV from
RT Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT and 11 new ORFs.";
RL Yeast 13:65-71(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6] {ECO:0007744|PDB:2WSI}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=20359485; DOI=10.1016/j.jmb.2010.03.040;
RA Leulliot N., Blondeau K., Keller J., Ulryck N., Quevillon-Cheruel S.,
RA van Tilbeurgh H.;
RT "Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD.";
RL J. Mol. Biol. 398:641-646(2010).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC form flavin adenine dinucleotide (FAD) coenzyme.
CC {ECO:0000269|PubMed:7799934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000269|PubMed:7799934};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000269|PubMed:7799934}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7799934}.
CC -!- MISCELLANEOUS: FAD1 is essential for growth.
CC {ECO:0000269|PubMed:7799934}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. FAD1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12331; AAA65730.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96444.1; -; Genomic_DNA.
DR EMBL; Z74093; CAA98604.1; -; Genomic_DNA.
DR EMBL; AY558157; AAS56483.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11811.1; -; Genomic_DNA.
DR PIR; S47906; S47906.
DR RefSeq; NP_010239.1; NM_001180104.1.
DR PDB; 2WSI; X-ray; 1.90 A; A=1-306.
DR PDBsum; 2WSI; -.
DR AlphaFoldDB; P38913; -.
DR SMR; P38913; -.
DR BioGRID; 32014; 188.
DR DIP; DIP-4735N; -.
DR IntAct; P38913; 1.
DR STRING; 4932.YDL045C; -.
DR MaxQB; P38913; -.
DR PaxDb; P38913; -.
DR PRIDE; P38913; -.
DR TopDownProteomics; P38913; -.
DR EnsemblFungi; YDL045C_mRNA; YDL045C; YDL045C.
DR GeneID; 851516; -.
DR KEGG; sce:YDL045C; -.
DR SGD; S000002203; FAD1.
DR VEuPathDB; FungiDB:YDL045C; -.
DR eggNOG; KOG2644; Eukaryota.
DR GeneTree; ENSGT00390000007266; -.
DR HOGENOM; CLU_056971_0_1_1; -.
DR InParanoid; P38913; -.
DR OMA; LLHWKLA; -.
DR BioCyc; MetaCyc:YDL045C-MON; -.
DR BioCyc; YEAST:YDL045C-MON; -.
DR BRENDA; 2.7.7.2; 984.
DR Reactome; R-SCE-196843; Vitamin B2 (riboflavin) metabolism.
DR UniPathway; UPA00277; UER00407.
DR EvolutionaryTrace; P38913; -.
DR PRO; PR:P38913; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38913; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:SGD.
DR GO; GO:0006747; P:FAD biosynthetic process; IDA:SGD.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01507; PAPS_reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; FAD; Flavoprotein; FMN;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..306
FT /note="Flavin adenine dinucleotide synthase"
FT /id="PRO_0000100691"
FT BINDING 59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT BINDING 182..185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:2WSI"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 44..48
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2WSI"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2WSI"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2WSI"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:2WSI"
SQ SEQUENCE 306 AA; 35546 MW; 55BBB830163A457F CRC64;
MQLSKAAEMC YEITNSYLHI DQKSQIIAST QEAIRLTRKY LLSEIFVRWS PLNGEISFSY
NGGKDCQVLL LLYLSCLWEY FFIKAQNSQF DFEFQSFPMQ RLPTVFIDQE ETFPTLENFV
LETSERYCLS LYESQRQSGA SVNMADAFRD FIKIYPETEA IVIGIRHTDP FGEALKPIQR
TDSNWPDFMR LQPLLHWDLT NIWSFLLYSN EPICGLYGKG FTSIGGINNS LPNPHLRKDS
NNPALHFEWE IIHAFGKDAE GERSSAINTS PISVVDKERF SKYHDNYYPG WYLVDDTLER
AGRIKN
