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Database: UniProt
Entry: A0A0N5CJD5_THECL
LinkDB: A0A0N5CJD5_THECL
Original site: A0A0N5CJD5_THECL 
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
//
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