ID A0A090L0B7_STRRB Unreviewed; 332 AA.
AC A0A090L0B7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=SRAE_1000139600 {ECO:0000313|EMBL:CEF63131.1,
GN ECO:0000313|WBParaSite:SRAE_1000139600.1,
GN ECO:0000313|WormBase:SRAE_1000139600};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63131.1};
RN [1] {ECO:0000313|EMBL:CEF63131.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000139600.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF63131.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000139600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609528; CEF63131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L0B7; -.
DR STRING; 34506.A0A090L0B7; -.
DR EnsemblMetazoa; SRAE_1000139600.1; SRAE_1000139600.1; WBGene00258001.
DR WBParaSite; SRAE_1000139600.1; SRAE_1000139600.1; WBGene00258001.
DR WormBase; SRAE_1000139600; SRP07387; WBGene00258001; -.
DR OrthoDB; 5475801at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; 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:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 140..208
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT DOMAIN 224..296
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 332 AA; 38941 MW; 0CA79689291FA9BD CRC64;
MKSYVEEKVV SLSRKFYYQN QSNFIDEHLT KCLNILLKKY PKIKFSIISN LSLLNGNLIV
VTVESLNHDL SYLDDASNFF YETTKEFTLS HNDIISNDIL NMEYFISTLS DEKCDEELKK
KISKSFQDIF YILSMYSLSQ IFISFNGGKD CTLALHLFSL CLKSKYPTLR DSIQAFIHKT
SEEFTEIEPF INKVCPLYNI SKHVYSLSMK ESLSKLKKDF PTVFPIIMGT RYMDPAGKYM
KSNICETDND WPKLLRVCPI FDWNYHEVWR VIKTLNIPYC SLYDEGYTSL GEKRSTIKNE
ELVRKENGNI IGYYPAYKLK NCELERVNRK II
//
