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Q58579

- RIBL_METJA

UniProt

Q58579 - RIBL_METJA

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Protein

FAD synthase

Gene
ribL, MJ1179
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3-phosphate cytidylyltransferase, as previously annotated in the complete genome.1 Publication

Catalytic activityi

ATP + FMN = diphosphate + FAD.1 Publication

Cofactori

Divalent metal cations. The best activity is observed with Co2+, where the activity is 4 and 2.5 times greater than that with Mg2+ and Mn2+, respectively.1 Publication

Enzyme regulationi

Is inhibited by the product PPi.1 Publication

Kineticsi

  1. KM=25 µM for ATP1 Publication
  2. KM=63 µM for FMN
  3. KM=480 µM for CTP

Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates

Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231ATP; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 112ATP By similarity
Nucleotide bindingi15 – 184ATP By similarity
Nucleotide bindingi93 – 964ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. CTP binding Source: UniProtKB
  3. FMN adenylyltransferase activity Source: UniProtKB
  4. FMN binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16487.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthase (EC:2.7.7.2)
Alternative name(s):
FMN adenylyltransferase
Flavin adenine dinucleotide synthase
Gene namesi
Name:ribL
Ordered Locus Names:MJ1179
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261C → S: 2-fold increase in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication
Mutagenesisi143 – 1431C → S: Nearly no change in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 149149FAD synthaseUniRule annotationPRO_0000107202Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ1179.

Structurei

3D structure databases

ProteinModelPortaliQ58579.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0615.
KOiK14656.
OMAiFAKKHAD.
PhylomeDBiQ58579.

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.

Q58579-1 [UniParc]FASTAAdd to Basket

« Hide

MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP    50
IIPEEQRREM VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD 100
EETLKKELAK YNLYPEIVRF RGYKKCPFHS SFDIVKEIIR RFCNKEIKI 149
Length:149
Mass (Da):17,288
Last modified:November 1, 1996 - v1
Checksum:i55FD11671ED94594
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99182.1.
PIRiB64447.
RefSeqiNP_248173.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99182; AAB99182; MJ_1179.
GeneIDi1452077.
KEGGimja:MJ_1179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99182.1 .
PIRi B64447.
RefSeqi NP_248173.1. NC_000909.1.

3D structure databases

ProteinModelPortali Q58579.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ1179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB99182 ; AAB99182 ; MJ_1179 .
GeneIDi 1452077.
KEGGi mja:MJ_1179.

Phylogenomic databases

eggNOGi COG0615.
KOi K14656.
OMAi FAKKHAD.
PhylomeDBi Q58579.

Enzyme and pathway databases

UniPathwayi UPA00277 ; UER00407 .
BioCyci MetaCyc:MONOMER-16487.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_02115. FAD_synth_arch.
InterProi IPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Archaeal RibL: a new FAD synthetase that is air sensitive."
    Mashhadi Z., Xu H., Grochowski L.L., White R.H.
    Biochemistry 49:8748-8755(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ENZYME REGULATION, GENE NAME, PATHWAY, SUBUNIT, MUTAGENESIS OF CYS-126 AND CYS-143.
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Entry informationi

Entry nameiRIBL_METJA
AccessioniPrimary (citable) accession number: Q58579
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Alkylation of both Cys-126 and Cys-143 results in complete loss of enzymatic activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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