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Protein

FAD synthase

Gene

ribL

Organism
Thermococcus sibiricus (strain MM 739 / DSM 12597)
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 bindingi14 – 152ATPUniRule annotation
Nucleotide bindingi19 – 224ATPUniRule annotation
Nucleotide bindingi98 – 1014ATPUniRule 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

BioCyciTSIB604354:GHMS-1366-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:TSIB_1332
OrganismiThermococcus sibiricus (strain MM 739 / DSM 12597)
Taxonomic identifieri604354 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
ProteomesiUP000009079: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148FAD synthasePRO_0000406285Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi604354.TSIB_1332.

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.

C6A439-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKKKKIRVV TGGVFDILHV GHIHFLKQAK ELGDELVVIV AHDKTVEERK
60 70 80 90 100
GRRPINSMYE RAEVLKALKM VDEVVIGEPN CISFEIVKQL NPDIIALGPD
110 120 130 140
QNFDVSALKE ELKKKNINAE VIRIPYAYKS DVAKTSKIIQ KIVETFCE
Length:148
Mass (Da):16,783
Last modified:September 1, 2009 - v1
Checksum:iEDF77BDFAC2D08F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001463 Genomic DNA. Translation: ACS90384.1.
RefSeqiWP_015849602.1. NC_012883.1.
YP_002994733.1. NC_012883.1.

Genome annotation databases

EnsemblBacteriaiACS90384; ACS90384; TSIB_1332.
GeneIDi8096333.
KEGGitsi:TSIB_1332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001463 Genomic DNA. Translation: ACS90384.1.
RefSeqiWP_015849602.1. NC_012883.1.
YP_002994733.1. NC_012883.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi604354.TSIB_1332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS90384; ACS90384; TSIB_1332.
GeneIDi8096333.
KEGGitsi:TSIB_1332.

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciTSIB604354:GHMS-1366-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. "Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
    Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
    Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MM 739 / DSM 12597.

Entry informationi

Entry nameiRIBL_THESM
AccessioniPrimary (citable) accession number: C6A439
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: September 1, 2009
Last modified: February 4, 2015
This is version 38 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.