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Protein

FAD synthase

Gene

ribL

Organism
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.UniRule annotation

Catalytic activityi

ATP + FMN = diphosphate + FAD.UniRule annotation

Cofactori

a divalent metal cationUniRule annotation

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 102ATPUniRule annotation
Nucleotide bindingi14 – 174ATPUniRule annotation
Nucleotide bindingi90 – 934ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. FMN adenylyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-HAMAP
  2. FMN metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciHSAL478009:GJVF-647-MONOMER.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthaseUniRule annotation (EC:2.7.7.2UniRule annotation)
Alternative name(s):
FMN adenylyltransferaseUniRule annotation
Flavin adenine dinucleotide synthaseUniRule annotation
Gene namesi
Name:ribLUniRule annotation
Ordered Locus Names:OE_2139R
OrganismiHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Taxonomic identifieri478009 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
ProteomesiUP000001321: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146FAD synthasePRO_0000406237Add
BLAST

Proteomic databases

PRIDEiB0R450.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi478009.OE2139R.

Structurei

3D structure databases

ProteinModelPortaliB0R450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal FAD synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02115. FAD_synth_arch.
InterProiIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

B0R450-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRVVAQGTF DLIHPGHVHY LEDAAAMGDE LHVILARREN VTHKDPPVLP
60 70 80 90 100
NRQRRDVVAA LDPVDHARIG HPEDIFAPIE AIDPDVIALG FDQHHDAAAI
110 120 130 140
EAELADRGLD CAVERASPRE ARYDDEVLSS GDIADRVLAQ RGDSDP
Length:146
Mass (Da):16,002
Last modified:April 8, 2008 - v1
Checksum:i6180FB34D13242F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774415 Genomic DNA. Translation: CAP13515.1.
RefSeqiYP_001688863.1. NC_010364.1.

Genome annotation databases

EnsemblBacteriaiCAP13515; CAP13515; OE_2139R.
GeneIDi5953509.
KEGGihsl:OE2139R.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM774415 Genomic DNA. Translation: CAP13515.1.
RefSeqiYP_001688863.1. NC_010364.1.

3D structure databases

ProteinModelPortaliB0R450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi478009.OE2139R.

Proteomic databases

PRIDEiB0R450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP13515; CAP13515; OE_2139R.
GeneIDi5953509.
KEGGihsl:OE2139R.

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciHSAL478009:GJVF-647-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02115. FAD_synth_arch.
InterProiIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
    Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
    Genomics 91:335-346(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29341 / DSM 671 / R1.

Entry informationi

Entry nameiRIBL_HALS3
AccessioniPrimary (citable) accession number: B0R450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: April 8, 2008
Last modified: February 4, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.