ID W7BTW6_9LIST Unreviewed; 253 AA.
AC W7BTW6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00012393};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
GN ORFNames=PCORN_14349 {ECO:0000313|EMBL:EUJ26701.1};
OS Listeria cornellensis FSL F6-0969.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ26701.1, ECO:0000313|Proteomes:UP000019254};
RN [1] {ECO:0000313|EMBL:EUJ26701.1, ECO:0000313|Proteomes:UP000019254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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: Belongs to the RibF family.
CC {ECO:0000256|ARBA:ARBA00010214}.
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:EUJ26701.1}.
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DR EMBL; AODE01000029; EUJ26701.1; -; Genomic_DNA.
DR RefSeq; WP_036081076.1; NZ_AODE01000029.1.
DR AlphaFoldDB; W7BTW6; -.
DR STRING; 1265820.PCORN_14349; -.
DR PATRIC; fig|1265820.5.peg.2834; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000019254; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd02064; FAD_synthetase_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF06574; FAD_syn; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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}; Kinase {ECO:0000313|EMBL:EUJ26701.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..166
FT /note="FAD synthetase"
FT /evidence="ECO:0000259|Pfam:PF06574"
SQ SEQUENCE 253 AA; 28608 MW; 91A026C37A094546 CRC64;
MEIFQVKDRL PDSEEPVVLV IGKFDGVHKG HQHLLKRAKS FCKAGEKLAI VCFTPHPLWA
LKKNPVYQRA ITPDVEKFHW LAHFGVNKVY NIGFTEQYAE TSAETFIREH LNGLNLAHIA
VGESFNFGKG RDSDVDLLMD LCGERSVPVT EISFVRDGAN HKVSATDIRA ALYEGNFEEA
ERLLGHPYFI EGDVRTKNGA YLLTGLDDFV LPKAGKYQVF VCGERTEIQV LENGEIKIPQ
QVKHIRIQFD TIQ
//
