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Database: UniProt
Entry: A0A0D9Y6A7_9ORYZ
LinkDB: A0A0D9Y6A7_9ORYZ
Original site: A0A0D9Y6A7_9ORYZ 
ID   A0A0D9Y6A7_9ORYZ        Unreviewed;       461 AA.
AC   A0A0D9Y6A7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G11420.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM01G11420.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM01G11420.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D9Y6A7; -.
DR   STRING; 40148.A0A0D9Y6A7; -.
DR   EnsemblPlants; OGLUM01G11420.1; OGLUM01G11420.1; OGLUM01G11420.
DR   Gramene; OGLUM01G11420.1; OGLUM01G11420.1; OGLUM01G11420.
DR   eggNOG; KOG2644; Eukaryota.
DR   HOGENOM; CLU_029083_1_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
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; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          239..423
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   461 AA;  50705 MW;  957231EFD0191C67 CRC64;
     MEIDRAVRGS SDRRLRTKYD NAVYVVQRAF ALYPFEEVAF SFNGGKDSTV LLHLLRAGYY
     LHKSSSDGEV EMNTIQNCPV RTIYFESPCA FPEINSFTYE TVSTYGLPLE TIHSDFKSGL
     EGLLKERPTK AIFIGTRIGD PNAVGQEQFS PSSPGWPPFM RVNPILDWSY RYTSIGSIYD
     TVPNALLSDS TTGKSFRPAY MLSDGRLERA GRTKKNISSV SSNGTNSTEV EQTISRSASI
     IVVGDEILFG TVEDKLGAGL CKKLHAIGWR VSHVAVVSNE IDSVAEEVER CKSTDDMVFL
     VGGLGPLHSD ISLAGVAKAF GVRLAPDEEF EEYLSQLIGD NYTGDRNEIK CKNVVILAAT
     NVDELETEWG CLLDTQESGL VMAKSFVSKH LCTSLLDVKI APVVAKLCID FSDLYIGCYR
     ISRSGPLVVS FLGKDNQRVE AAAEKLTNSF EGQFSQVDSC K
//
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