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Database: UniProt
Entry: G0VK53_NAUCC
LinkDB: G0VK53_NAUCC
Original site: G0VK53_NAUCC 
ID   G0VK53_NAUCC            Unreviewed;       311 AA.
AC   G0VK53;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00012393};
DE            EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
DE   AltName: Full=FAD pyrophosphorylase {ECO:0000256|ARBA:ARBA00031145};
DE   AltName: Full=FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00031871};
GN   Name=NCAS0I02190 {ECO:0000313|EMBL:CCC71887.1};
GN   OrderedLocusNames=NCAS_0I02190 {ECO:0000313|EMBL:CCC71887.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71887.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC71887.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001332};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004726}.
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DR   EMBL; HE576760; CCC71887.1; -; Genomic_DNA.
DR   RefSeq; XP_003678229.1; XM_003678181.1.
DR   AlphaFoldDB; G0VK53; -.
DR   STRING; 1064592.G0VK53; -.
DR   GeneID; 11525537; -.
DR   KEGG; ncs:NCAS_0I02190; -.
DR   eggNOG; KOG2644; Eukaryota.
DR   HOGENOM; CLU_056971_0_1_1; -.
DR   InParanoid; G0VK53; -.
DR   OMA; LLHWKLA; -.
DR   OrthoDB; 5475801at2759; -.
DR   Proteomes; UP000001640; Chromosome 9.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR23293:SF9; FAD SYNTHASE; 1.
DR   PANTHER; PTHR23293; FAD SYNTHETASE-RELATED FMN ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          56..232
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   311 AA;  36116 MW;  5AD2B4A65CE357E9 CRC64;
     MGLGEISELC YRITESYLQL PNRTDIITET KDAIRLTREY LLDDIFTRWS PINGQISFSY
     NGGKDCQVLL LLYLSCLWEF FYINGKTSQF DYEYQKFPMK LLPTVFIDQD ATFITLEKFI
     SETSQRYSLS LYESRREVSK NQNMADSFRD FLKIYPETEA IVIGIRHTDP YGESLKPIQK
     TDSNWPEFIR LQPLLHWKLA SIWSFLLFSN EPICGLYGVG FTSIGSMEST VPNPYLSKKG
     NDVLPLQFEW EINNAFGKEK EGETKTVHVS NLEESDQEWL ATVTDSDYYP GWYLIDDSIE
     RAGRIKKGKG K
//
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