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Database: UniProt
Entry: E3KT79_PUCGT
LinkDB: E3KT79_PUCGT
Original site: E3KT79_PUCGT 
ID   E3KT79_PUCGT            Unreviewed;       244 AA.
AC   E3KT79;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 46.
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   ORFNames=PGTG_13875 {ECO:0000313|EMBL:EFP87504.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP87504.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; DS178307; EFP87504.2; -; Genomic_DNA.
DR   RefSeq; XP_003331923.2; XM_003331875.2.
DR   AlphaFoldDB; E3KT79; -.
DR   STRING; 418459.E3KT79; -.
DR   EnsemblFungi; EFP87504; EFP87504; PGTG_13875.
DR   GeneID; 10538403; -.
DR   KEGG; pgr:PGTG_13875; -.
DR   VEuPathDB; FungiDB:PGTG_13875; -.
DR   eggNOG; KOG2644; Eukaryota.
DR   HOGENOM; CLU_056971_0_1_1; -.
DR   InParanoid; E3KT79; -.
DR   OrthoDB; 5475801at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006747; P:FAD biosynthetic process; IBA:GO_Central.
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; 2.
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:UP000008783};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          55..128
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   DOMAIN          142..214
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   244 AA;  27200 MW;  10C983707FAE8A15 CRC64;
     MANPDSLRSR FGKPDADRVY QLAHSPTPTQ LSLQIKHALE IIELAIVRFG VDGLSISFNG
     GKDSTVLVHL FAAALYRNSS IPTSSEPEPN LKISGLYIRC QSPFAEVDEF VNHCQTIYNI
     DLMTVDNSLK NGLGAFLAER PSIKAILIGT RATDPNGGSL TDFDPTDSDW PSIIRVHPIL
     DWGYSHVWEF LQKLEVDWCK LYNSGYTSLG SSFNTFKNPF LETDDGWKAA WELSDGRNER
     AGRM
//
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