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Protein

FAD synthase

Gene

ribL

Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
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

BioCyciMBUR259564:GHBZ-439-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:Mbur_0427
OrganismiMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
Taxonomic identifieri259564 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides
ProteomesiUP000001979 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143FAD synthasePRO_0000406252Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi259564.Mbur_0427.

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.

Q12YR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRVLATGTF DLLHPGHVFF LRQARSFGDE LYVLVARDSM IKHKAQPIVP
60 70 80 90 100
EGQRLKMISA FGVVDKALLG SESDIFEPLK EINPDIIVLG HDQFFDTGEL
110 120 130 140
EKNLGERGFK AKVVRIDDAM KCELCSSGRI IKRVLERYGQ NEE
Length:143
Mass (Da):16,148
Last modified:August 22, 2006 - v1
Checksum:iA725DEE6FC362139
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE51415.1.
RefSeqiYP_565165.1. NC_007955.1.

Genome annotation databases

EnsemblBacteriaiABE51415; ABE51415; Mbur_0427.
GeneIDi3996820.
KEGGimbu:Mbur_0427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE51415.1.
RefSeqiYP_565165.1. NC_007955.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi259564.Mbur_0427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE51415; ABE51415; Mbur_0427.
GeneIDi3996820.
KEGGimbu:Mbur_0427.

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciMBUR259564:GHBZ-439-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Entry informationi

Entry nameiRIBL_METBU
AccessioniPrimary (citable) accession number: Q12YR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: August 22, 2006
Last modified: April 1, 2015
This is version 58 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, Reference 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.