RIBL_HALSA
ID RIBL_HALSA Reviewed; 146 AA.
AC Q9HRB2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 {ECO:0000255|HAMAP-Rule:MF_02115}; OrderedLocusNames=VNG_0777G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG19246.1; -; Genomic_DNA.
DR PIR; B84235; B84235.
DR RefSeq; WP_010902542.1; NC_002607.1.
DR AlphaFoldDB; Q9HRB2; -.
DR SMR; Q9HRB2; -.
DR STRING; 64091.VNG_0777G; -.
DR PaxDb; Q9HRB2; -.
DR EnsemblBacteria; AAG19246; AAG19246; VNG_0777G.
DR GeneID; 5953509; -.
DR GeneID; 62886369; -.
DR KEGG; hal:VNG_0777G; -.
DR PATRIC; fig|64091.14.peg.597; -.
DR HOGENOM; CLU_034585_2_1_2; -.
DR InParanoid; Q9HRB2; -.
DR OMA; FAKKHAD; -.
DR OrthoDB; 79845at2157; -.
DR PhylomeDB; Q9HRB2; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000554; 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 3: Inferred from homology;
KW ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..146
FT /note="FAD synthase"
FT /id="PRO_0000406236"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
SQ SEQUENCE 146 AA; 16002 MW; 6180FB34D13242F8 CRC64;
MTRVVAQGTF DLIHPGHVHY LEDAAAMGDE LHVILARREN VTHKDPPVLP NRQRRDVVAA
LDPVDHARIG HPEDIFAPIE AIDPDVIALG FDQHHDAAAI EAELADRGLD CAVERASPRE
ARYDDEVLSS GDIADRVLAQ RGDSDP
