ID G1NXS9_MYOLU Unreviewed; 550 AA.
AC G1NXS9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=FLAD1 {ECO:0000313|Ensembl:ENSMLUP00000002192.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000002192.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000002192.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000002192.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AAPE02030007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1NXS9; -.
DR STRING; 59463.ENSMLUP00000002192; -.
DR Ensembl; ENSMLUT00000002412.2; ENSMLUP00000002192.2; ENSMLUG00000002412.2.
DR eggNOG; KOG2644; Eukaryota.
DR GeneTree; ENSGT00390000007266; -.
DR HOGENOM; CLU_030805_8_0_1; -.
DR InParanoid; G1NXS9; -.
DR OMA; NSHFLCK; -.
DR TreeFam; TF314056; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036620}.
FT DOMAIN 77..238
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 550 AA; 60815 MW; 07E745194FD43581 CRC64;
PALPHFPFWL LQVASTPDPL FPGYGPQCPL DLAGLPCLRP LFGGLGGYRR ALQRGREGRT
MASRASAPPP GRSVTAGIII VGDEILKGHT QDTNTYFLCR TLRSLGVQVC RVSVVPDEVA
TIAAEITSFS SRFTHVLTAG GIGPTHDDVT FEAVAQAFGD ELKPHPELQA AIQALGRQGW
EKLSLVPSSA RLHYGTDPHT GRPFKFPLVS VRNVYLFPGI PELLRRVLEG LKGLFQNTAV
QFHLRELYVA ADEASIAPIL AEAQAHFGHR LGLGSYPDWG SNYYQVKVTL DSQEEGPLEE
CLAYLTARLP RGSLVPYVPN AMEQASEAVY KLAKSGSSLG KKVASALQTI ETALARYRLT
QLCVGFNGGK DCTALLHLVH AAVQRQCPGT QEPLQILYIR SISPFPELEQ FLQDTIKRYN
LRVLEAEGEM KKALSQLRAQ HPQLEAALMG TRRTDPSSCS LCPFSPTDPG WPSFMRINPL
LDWTYRDIWD FLRQLFVPYC ILYDRGYTSL GSRENTVQNP ALKYLGPGGQ PTYRPAYLLE
NEDEERNSRL
//
