ID A0A0N5CJD5_THECL Unreviewed; 554 AA.
AC A0A0N5CJD5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=TCLT_LOCUS138 {ECO:0000313|EMBL:VDM94983.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000013701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000013701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM94983.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; UYYF01000008; VDM94983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N5CJD5; -.
DR STRING; 103827.A0A0N5CJD5; -.
DR WBParaSite; TCLT_0000013701-mRNA-1; TCLT_0000013701-mRNA-1; TCLT_0000013701.
DR OMA; NSHFLCK; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
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; PF00994; MoCF_biosynth; 1.
DR Pfam; PF01507; PAPS_reduct; 2.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..219
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 554 AA; 63375 MW; 137C8779F9065FAA CRC64;
MTLQSKADLR ERYISDFPQM IANLNRKTAG VIVIGDEILK GITQDVNSIF FCKELHRKGV
LLKKISVVSD DVEDIAREVK QFSRRFDIVL SSGGIGPTHD DRTYTGLAIA FDDELTIRKE
MKEWMKYFMC KMSKIIPDGG LERMCTVSIH LKLLTVITES CQTPTTFEIH YIPKTAHLLW
SERRVFPLVQ MRNVYAFPGI PKFCTDAFKE FEDSLFPSYA TKPFHSSTLH IKTTELQFSD
IMMKTAEKYG AKNVSIGSYP TTSNNYYKTK LLVESESADL VEKVVQDLKT NLRDQVTYFD
EEPWIDTVQK FSVFREKELE KNDGGFIRRL DDAMQCIDEI VSQKELDELC ISFNGGKDCT
VVLHLLRIAI DKKYGPQQTI LGFHIVCGDS FPEVNQFIID TAKWSVQYLR TKFCLFEKFL
YNIMILEISG PLKAGLLQLK DMRPKLKCVF MGSRETDPSA SYIKSKCQST DPGWPSYLRV
CPILDWSYND VWRTLRGICI PYCSLYDLGY TSLGERDTTR KNDALKIVDG KGCTVGYHPA
YMLGAATLER SGRS
//