ID T1HF00_RHOPR Unreviewed; 503 AA.
AC T1HF00;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC002622-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC002622-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) 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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; ACPB03013538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HF00; -.
DR STRING; 13249.T1HF00; -.
DR EnsemblMetazoa; RPRC002622-RA; RPRC002622-PA; RPRC002622.
DR VEuPathDB; VectorBase:RPRC002622; -.
DR eggNOG; KOG2644; Eukaryota.
DR HOGENOM; CLU_030805_8_0_1; -.
DR InParanoid; T1HF00; -.
DR OMA; NSHFLCK; -.
DR OrthoDB; 5475801at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00885; cinA; 1.
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; 1.
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:UP000015103};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..189
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 503 AA; 57689 MW; 191FAD38312CEDBC CRC64;
LSFYLVLEFT ERMAARSAGV IVIGDEVLKG QVADSNVHFL AKKLHSLGIK LCKVSIIPDD
IEIIAKEVAE FSTKYDQVIT SGGIGPTHDD VTYEGVGAAF LQPMIVNQEL LIYWSWFNRD
PPGSEQREST VKMATIPRDA VIHYAHLNTT LVPEEKFPVI TVNNVCILPG LPKYFRAIFN
ALEGTYFRNS GLKFHVRRMY LDVYESEFAH YLNDAVKKYK DVTFGSYPKL NNPFFKTVIT
LECQEEQLVE QAYSFFESRL NKDWIAEQGE LLGNSWNRIK ELLDADEAEA MSLTRCLKRS
IEIIEKCLDE YQTSEVFLSF NGGKDCTVLV HLVQSLLLKR FNNRTEFPEL NAVYIRTESP
FKEVEDFIRE TASRYNLKLI IEDGPLKKGI QKVLSGRQDF KVSILGIRRT DPSVYCRIFT
DICWGNLIRV SPLLDWSYQD IWTYLKELNV PYCPLYDKGY TSLGSTVNSV PNPALKYVDE
DGTVKYRPAF CLQDEHLERV GRQ
//