ID Q4RIB2_TETNG Unreviewed; 518 AA.
AC Q4RIB2;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00015431, ECO:0000256|PIRNR:PIRNR036620};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393, ECO:0000256|PIRNR:PIRNR036620};
DE AltName: Full=FAD pyrophosphorylase {ECO:0000256|ARBA:ARBA00031145, ECO:0000256|PIRNR:PIRNR036620};
DE AltName: Full=FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00031871, ECO:0000256|PIRNR:PIRNR036620};
DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000256|ARBA:ARBA00031676, ECO:0000256|PIRNR:PIRNR036620};
GN ORFNames=GSTENG00033959001 {ECO:0000313|EMBL:CAG11870.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG11870.1};
RN [1] {ECO:0000313|EMBL:CAG11870.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG11870.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC form flavin adenine dinucleotide (FAD) coenzyme.
CC {ECO:0000256|ARBA:ARBA00003316, ECO:0000256|PIRNR:PIRNR036620}.
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 ECO:0000256|PIRNR:PIRNR036620};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR036620};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726, ECO:0000256|PIRNR:PIRNR036620}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS reductase
CC family. FAD1 subfamily. {ECO:0000256|ARBA:ARBA00006749,
CC ECO:0000256|PIRNR:PIRNR036620}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589, ECO:0000256|PIRNR:PIRNR036620}.
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:CAG11870.1}.
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DR EMBL; CAAE01015044; CAG11870.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4RIB2; -.
DR KEGG; tng:GSTEN00033959G001; -.
DR UniPathway; UPA00277; UER00407.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR012183; FAD_synth_MoaB/Mog-bd.
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 PIRSF; PIRSF036620; MPTbdFAD; 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, ECO:0000256|PIRNR:PIRNR036620};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR036620};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR036620};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR036620};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036620};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR036620};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036620}.
FT DOMAIN 41..208
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAG11870.1"
SQ SEQUENCE 518 AA; 58176 MW; 8F7A0B9F329D3014 CRC64;
MLSRQAVRVR RLAAHLCKAM SSDQQASSPS FVSNGEAPTA AILIIGDEIL KGHTLDTNSA
FLTRALRKLG VSVRRITVIP DIQEIIAKEV ALLSAQYTHL ITSGGIGPTH DDVTFESVAM
AFQEELYPHP ELTRLVQEFF GVVDRNSTTF KLAMVPRSAK LNYGTDPQTG KPLRYPLVSV
RNVYIFPGIP SLMERAFKGL EHLFAGSGTT FHSREVFVDA DETEIAPVLT KLQSCWGRKV
ALGSYPDWLS NYHRVRLVLD SQSQEELEKA RARLLDELPK GSVVALVTDP VSVATAEVYA
LANNGTPLGE KVKSALRTIE AALDRYATEE ICVGFNGGKD CTALLHLYYA ALKRRYPDGK
DRVKALYIRI VSPFPEMERF LQDTIKRYDL ELISVEGSIR QALSEVQERR PGLKAVLMGT
RRSDPYSLTL TPMCPTDPGW PDYMRVNPLL DWTYHDIWSF LRTLFVPYCI LYDKGYTSLG
SMDNTCRNPS LQKVDERGVT RYKPAYLLEN EEEERNSR
//
