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Database: UniProt
Entry: V6U372_GIAIN
LinkDB: V6U372_GIAIN
Original site: V6U372_GIAIN 
ID   V6U372_GIAIN            Unreviewed;       616 AA.
AC   V6U372;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=GSB_150799 {ECO:0000313|EMBL:ESU45082.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU45082.1, ECO:0000313|Proteomes:UP000018040};
RN   [1] {ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA   Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA   Nash T.;
RT   "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT   Pig).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESU45082.1, ECO:0000313|Proteomes:UP000018040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS {ECO:0000313|EMBL:ESU45082.1,
RC   ECO:0000313|Proteomes:UP000018040};
RX   PubMed=24307482; DOI=10.1093/gbe/evt197;
RA   Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA   Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA   Nash T.E.;
RT   "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT   Pig).";
RL   Genome Biol. Evol. 5:2498-2511(2013).
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:ESU45082.1}.
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DR   EMBL; AHHH01000011; ESU45082.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6U372; -.
DR   EnsemblProtists; ESU45082; ESU45082; GSB_150799.
DR   VEuPathDB; GiardiaDB:DHA2_150166; -.
DR   VEuPathDB; GiardiaDB:GL50581_818; -.
DR   VEuPathDB; GiardiaDB:GL50803_0016269; -.
DR   VEuPathDB; GiardiaDB:QR46_0418; -.
DR   Proteomes; UP000018040; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          230..308
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          361..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68603 MW;  D1C366B7753C8B14 CRC64;
     MSSHHIYPEF LFSSPKKEET ILLNPDSVIP SGSEWFPECK SILEFAQKAT NSTNVFIQNR
     ISPSSTTVNI SSISHQADCL SSTHSTNVTE HIANNNSTSS TQLSSRLSDS PTTNDALELQ
     FAQKINQALI VIRMAMRQYR KLAFSFNGGK DNTVVLYLIR AACLQAVLEE NSDFEGTTPH
     ELLRSRFVFF YVHNEVQIKQ VMKFMCLIDH EQNLGTVVYA GTGFKNCIIN FYNDYRPDAV
     FMGVRSTDPN GKTTIFSHCS PSWPQFMRVC PILYWSYVDV WDFLKRFRIH YCTLYDQGYT
     SLGAATHTIK HPTLRDGTIM HRRIASMVNE PQFSTISGNT HTGKQTVQQI THIFTSKVSL
     APHGSNSNPH DRSNQQNWNG SPTIDDKCTS AKVLVKQLMN QAPSVKRPKN EHCGSKTLLL
     TNYLSRGVTS ASPTKDTVAN TTTSPSTNLR LKTSASIPTL ESTTDEEIEQ APLSTITPSF
     AVDSSNSSMI SQINVQNEYV QQPFVGCEPR TCHRLVSNPD INLSASEEYS ETGSIKSYIG
     DTGHEYYGSV TPQDICTYSG PRLVIDELIA RGVPTELLPP QFDPSEESGE IEDDICSASA
     IFLPVSEGED ERVNRT
//
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