RIBL_THEVO
ID RIBL_THEVO Reviewed; 142 AA.
AC Q979C2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115};
DE EC=2.7.7.2 {ECO:0000255|HAMAP-Rule:MF_02115};
DE AltName: Full=FMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_02115};
DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_02115};
GN Name=ribL; OrderedLocusNames=TV1239; ORFNames=TVG1279046;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH AMP.
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of the lipopolysaccharide core biosynthesis protein
RT from Thermoplasma volcanium GSS1.";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of the AMP portion of ATP to flavin
CC mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD)
CC coenzyme. {ECO:0000255|HAMAP-Rule:MF_02115}.
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:0000255|HAMAP-Rule:MF_02115};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02115};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_02115}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02115}.
CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_02115}.
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DR EMBL; BA000011; BAB60381.1; -; Genomic_DNA.
DR RefSeq; WP_010917473.1; NC_002689.2.
DR PDB; 3GLV; X-ray; 1.99 A; A/B=1-142.
DR PDBsum; 3GLV; -.
DR AlphaFoldDB; Q979C2; -.
DR SMR; Q979C2; -.
DR STRING; 273116.14325477; -.
DR DNASU; 1441355; -.
DR EnsemblBacteria; BAB60381; BAB60381; BAB60381.
DR GeneID; 1441355; -.
DR KEGG; tvo:TVG1279046; -.
DR eggNOG; arCOG01222; Archaea.
DR HOGENOM; CLU_034585_2_1_2; -.
DR OMA; FAKKHAD; -.
DR OrthoDB; 79845at2157; -.
DR PhylomeDB; Q979C2; -.
DR UniPathway; UPA00277; UER00407.
DR EvolutionaryTrace; Q979C2; -.
DR Proteomes; UP000001017; Chromosome.
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 GO; GO:0046444; P:FMN metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02115; FAD_synth_arch; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR024902; FAD_synth_RibL.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..142
FT /note="FAD synthase"
FT /id="PRO_0000406287"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.2"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.2"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3GLV"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3GLV"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3GLV"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3GLV"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:3GLV"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3GLV"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3GLV"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3GLV"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3GLV"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3GLV"
SQ SEQUENCE 142 AA; 16009 MW; B9A106F982D0022E CRC64;
MIRVMATGVF DILHLGHIHY LKESKKLGDE LVVVVARDST ARNNGKIPIF DENSRLALIS
ELKVVDRAIL GHEGDMMKTV IEVKPDIITL GYDQKFDEAE LQSKINKLGI TVKIVRISKY
DGQLNSSSSV RKKIMELIGE RY
