ID A0A0U5CX10_9EURY Unreviewed; 142 AA.
AC A0A0U5CX10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=FAD synthase {ECO:0000256|HAMAP-Rule:MF_02115};
DE EC=2.7.7.2 {ECO:0000256|HAMAP-Rule:MF_02115};
DE AltName: Full=FMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_02115};
DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000256|HAMAP-Rule:MF_02115};
GN Name=ribL {ECO:0000256|HAMAP-Rule:MF_02115,
GN ECO:0000313|EMBL:CQH52528.1};
GN ORFNames=HHUB_1853 {ECO:0000313|EMBL:CQH52528.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH52528.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
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:0000256|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:0000256|HAMAP-Rule:MF_02115};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02115};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|HAMAP-Rule:MF_02115}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02115}.
CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_02115}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02115}.
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DR EMBL; LN831302; CQH52528.1; -; Genomic_DNA.
DR RefSeq; WP_059056325.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5CX10; -.
DR STRING; 1407499.HHUB_1853; -.
DR GeneID; 26658530; -.
DR KEGG; hhb:Hhub_1853; -.
DR OrthoDB; 1912at2157; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000066737; Chromosome I.
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 CDD; cd02170; cytidylyltransferase; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02115};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_02115};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_02115};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02115};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02115};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_02115}; Reference proteome {ECO:0000313|Proteomes:UP000066737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02115}.
FT DOMAIN 6..133
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02115"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02115"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02115"
SQ SEQUENCE 142 AA; 15847 MW; 8048CD209827262D CRC64;
MRRVVAQGTF DLIHPGHIHY LEDAAAMGDE LHVIVARREN VTHKEPPVLP NRQRRDVVAA
LDAVDKARVG HESDIFAPIE DIDPDVIALG FDQHHDDDAI EAELAERGVD CSVERASARE
KRYDGELLST GTIIDRILEQ RG
//
