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Protein

FAD synthase

Gene

ribL

Organism
Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541) (Haloarcula mukohataei)
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

Pathway: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. FAD synthase (ribL)
This subpathway is part of the pathway FAD biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FAD from FMN, the pathway FAD biosynthesis and in Cofactor biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 122ATPUniRule annotation
Nucleotide bindingi16 – 194ATPUniRule annotation
Nucleotide bindingi92 – 954ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciHMUK485914:GCKD-1940-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:Hmuk_1909
OrganismiHalomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541) (Haloarcula mukohataei)
Taxonomic identifieri485914 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalomicrobium
ProteomesiUP000001746 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143FAD synthasePRO_0000406239Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi485914.Hmuk_1909.

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.

C7P4K0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTRDVVAQG TFDILHPGHV HYLREAKAMG DRLHVIVARS ENVTHKAPPV
60 70 80 90 100
VPDRQRVEMV EALDPVDYAR LGHAEDIFVP IEQIEPDVIA LGYDQHHEVE
110 120 130 140
GIETALDERG LDCEVRRAGP RKASEDEILS TGSIIEKILD ERS
Length:143
Mass (Da):16,018
Last modified:October 13, 2009 - v1
Checksum:iC93AA3BF9030A0F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001688 Genomic DNA. Translation: ACV48022.1.
RefSeqiWP_015762864.1. NC_013202.1.
YP_003177729.1. NC_013202.1.

Genome annotation databases

EnsemblBacteriaiACV48022; ACV48022; Hmuk_1909.
GeneIDi8411436.
KEGGihmu:Hmuk_1909.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001688 Genomic DNA. Translation: ACV48022.1.
RefSeqiWP_015762864.1. NC_013202.1.
YP_003177729.1. NC_013202.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi485914.Hmuk_1909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACV48022; ACV48022; Hmuk_1909.
GeneIDi8411436.
KEGGihmu:Hmuk_1909.

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciHMUK485914:GCKD-1940-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: ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541.

Entry informationi

Entry nameiRIBL_HALMD
AccessioniPrimary (citable) accession number: C7P4K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 13, 2009
Last modified: March 4, 2015
This is version 41 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.