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Database: UniProt
Entry: V6TIQ8_GIAIN
LinkDB: V6TIQ8_GIAIN
Original site: V6TIQ8_GIAIN 
ID   V6TIQ8_GIAIN            Unreviewed;       621 AA.
AC   V6TIQ8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=DHA2_150166 {ECO:0000313|EMBL:ESU38863.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU38863.1, ECO:0000313|Proteomes:UP000018320};
RN   [1] {ECO:0000313|Proteomes:UP000018320}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DH {ECO:0000313|Proteomes:UP000018320};
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:ESU38863.1, ECO:0000313|Proteomes:UP000018320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH {ECO:0000313|EMBL:ESU38863.1,
RC   ECO:0000313|Proteomes:UP000018320};
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:ESU38863.1}.
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DR   EMBL; AHGT01000008; ESU38863.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6TIQ8; -.
DR   EnsemblProtists; ESU38863; ESU38863; DHA2_150166.
DR   VEuPathDB; GiardiaDB:DHA2_150166; -.
DR   VEuPathDB; GiardiaDB:GL50581_818; -.
DR   VEuPathDB; GiardiaDB:GL50803_0016269; -.
DR   VEuPathDB; GiardiaDB:QR46_0418; -.
DR   Proteomes; UP000018320; 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          231..308
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          52..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  69526 MW;  341B1B6A754D88AE CRC64;
     MSTHHTYPEF LFSPPRKEEA ILLNPDSVIP KGSEWFPECK SILEFAQKAA NFTNGPTGDQ
     ESPQSATISA SNNPRQTSDL NPVRPPNEIR HMADNNDVRL NPSSTESTET PLVNDSLELQ
     FAQKIYQALV VIRVAMRQYR RLAFSFNGGK DNTVVLYLIR AACLQAVIEE NSDFESITPH
     ELLRSRFIFF YVHNEVQIKQ VMKFMCLIDH EQNLGTVVYL GTSFKNCIVN FYNDYHSDVV
     FMGVRSTDPN GKTTIFSHCS PSWPQFMRVC PILYWSYVDV WDFLKRFRIH YCTLYDQGYT
     SLGSATHTIK HPTLRDGAIM HRRIASMVHE PQFSAIGGST QTGKQTLQQI THIFTSRVSL
     STYGSNQESH TARDKNNQHN KNDIPVSNGR RTPIMPQVEW PTDQAPSAVK ERENEHPCSK
     TLLLTDYLSR GTMSVPSVKG TDGSTETPAS TKLRAMTSTS VASLVSTTDE EIEQGYPSMV
     TPSLVVDSSN SSMISQANIL HDRNMHQILA GRETHRHHRL LSNTDAALSA SEEYSEAGSI
     TSYMGDAGNE YYGSVTPQDV CAYSGPRLVI DELVARGVPT ELLPPQFDPS EEDGEIEDDL
     CSASAIFLPV SEGEDERINR V
//
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