ID A0A1V8TDV2_9PEZI Unreviewed; 293 AA.
AC A0A1V8TDV2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=B0A48_04816 {ECO:0000313|EMBL:OQO09418.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO09418.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO09418.1}.
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; NAJO01000010; OQO09418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TDV2; -.
DR STRING; 1507870.A0A1V8TDV2; -.
DR InParanoid; A0A1V8TDV2; -.
DR OrthoDB; 5475801at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 78..254
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 250..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 32945 MW; 78031459F012B74D CRC64;
MSPSTLLGIH SDTNGDTPTI IQSNPPALPD ICAKVDGRVE AFLNTEPRNE RTRHVQEQTR
ASLKIIQEAL ERYSSDELSI SYNGGKDCLV LLILYLAALH RYTTSPCPPK QTNGSPQAPA
RTPEPLPQTL RSVYILSPHP FPEVDAFVAT SAKTYHLSLA RYAKPMREAF TDYLANEPAI
RAIFVGTRRT DPHGSALKHF DPTDRGWPAF MRIHPVIDWH YAEIWAFIRE LDVPYCELYD
MGYTSLGGTT DTHPNPALRA DPGGGMEGKQ EKRVFRPAYE LEEDDEERLG RDR
//
