ID F7XRH3_TREPU Unreviewed; 275 AA.
AC F7XRH3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=FAD synthase {ECO:0000256|ARBA:ARBA00012393};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
GN Name=ribF {ECO:0000313|EMBL:AEH40814.1};
GN OrderedLocusNames=TPCCA_0888 {ECO:0000313|EMBL:AEH40814.1};
OS Treponema paraluiscuniculi (strain Cuniculi A).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545776 {ECO:0000313|EMBL:AEH40814.1, ECO:0000313|Proteomes:UP000008317};
RN [1] {ECO:0000313|EMBL:AEH40814.1, ECO:0000313|Proteomes:UP000008317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cuniculi A {ECO:0000313|EMBL:AEH40814.1,
RC ECO:0000313|Proteomes:UP000008317};
RX PubMed=21655244; DOI=10.1371/journal.pone.0020415;
RA Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S.,
RA Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K.,
RA Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.;
RT "Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A:
RT the loss of infectivity to humans is associated with genome decay.";
RL PLoS ONE 6:E20415-E20415(2011).
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}.
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DR EMBL; CP002103; AEH40814.1; -; Genomic_DNA.
DR RefSeq; WP_013945463.1; NC_015714.1.
DR AlphaFoldDB; F7XRH3; -.
DR KEGG; tpl:TPCCA_0888; -.
DR PATRIC; fig|545776.3.peg.895; -.
DR HOGENOM; CLU_048437_1_0_12; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000008317; Chromosome.
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; IPR015864; FAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF06574; FAD_syn; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Kinase {ECO:0000313|EMBL:AEH40814.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AEH40814.1};
KW Transferase {ECO:0000313|EMBL:AEH40814.1}.
FT DOMAIN 17..172
FT /note="FAD synthetase"
FT /evidence="ECO:0000259|Pfam:PF06574"
SQ SEQUENCE 275 AA; 30130 MW; FBF7C185C0737B05 CRC64;
MRIFRWSQLQ EGACIACDRG AAISVGGFDG PHRGHAFLFD KVFAAACAPV ADRARCTGLI
TFTHPPRKHK TSSYEGDLST LRLRLRYFRA RGFDFVVLID FSKDFARIPG GVFFNTLLRA
VRVCYLAVGV DFRCGHGLDT GVRELRRLGD AHSFVCDAVG HYTLEGVRVS SSAVRRAVRC
ADFESARRLL GRAFSLDGEV IPWQQSGGCA RTLCAERGRV SQTLPPEGEY AVRLVQGSGV
GLRAQLSVGS SLVQLRLGTE ALSRGREALD SIEFE
//
