ID A0A194UWC2_9PEZI Unreviewed; 347 AA.
AC A0A194UWC2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=VP1G_03242 {ECO:0000313|EMBL:KUI55919.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI55919.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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; KN714684; KUI55919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UWC2; -.
DR STRING; 694573.A0A194UWC2; -.
DR OrthoDB; 5475801at2759; -.
DR Proteomes; UP000078576; 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 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:UP000078576};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 228..316
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 38805 MW; 1D0C7C7685CCB1F2 CRC64;
MLHNHAANGT APSDANRGVD AIDTSPTLRQ VCLELQAKVD AFLAEDADTK LLRGLQAQVK
EAVGVIDEAL DRYRVGGRLI YEGNKVKNKK KKKKAHKSSH SVEELSLSYN GGKDCLVLLV
LILACLPRHY EETSSVPSSS SPTTTIPSTT TTTTTNITNA SINKLTAQIP TNTPAPPTPV
RPSTPQPFPS TLQSVYIVSP QPFAEVDDFV DESVAKYHLE LCRYSLPMRA ALEEYLKERP
RVKAVFVGTR RTDPHGASLT HFDQTDKDWP EFMRVHPVID WHYAEIWAFI RHLEIPYLSL
YDQGYTSLGG TKDTHPNPLL KREDEGEGFR PAYELLEDNE ERLGRDR
//
