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D9PX81

- RIBL_METTM

UniProt

D9PX81 - RIBL_METTM

Protein

FAD synthase

Gene

ribL

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (05 Oct 2010)
      Previous versions | rss
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    • Comment

    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

    Divalent metal cations.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei133 – 1331ATP; via amide nitrogenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 202ATPUniRule annotation
    Nucleotide bindingi24 – 274ATPUniRule annotation
    Nucleotide bindingi104 – 1074ATPUniRule 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

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMMAR79929:GH5J-1244-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:MTBMA_c12410
    OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri79929 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    ProteomesiUP000000345: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 161161FAD synthasePRO_0000406274Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the archaeal FAD synthase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000284153.
    KOiK14656.
    OMAiIVLGHDQ.

    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.

    D9PX81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRFSDKRTQ IKTVMATGTF DIIHPGHGFF LEEAKKLGGE NARLVVVLAR    50
    DSTVRARKRT PIIGEKQRLE VVMMLKPVDE AYLGSETDMF EIVHRLKPDI 100
    IAIGPDQKFD IDELRDELRR RGLECEVKRV GKYRRSELDS TCKIIKKIRK 150
    MEFDEDALKN C 161
    Length:161
    Mass (Da):18,664
    Last modified:October 5, 2010 - v1
    Checksum:i60C2822CE8D830C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001710 Genomic DNA. Translation: ADL58829.1.
    RefSeqiYP_003850142.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL58829; ADL58829; MTBMA_c12410.
    GeneIDi9704949.
    KEGGimmg:MTBMA_c12410.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001710 Genomic DNA. Translation: ADL58829.1 .
    RefSeqi YP_003850142.1. NC_014408.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL58829 ; ADL58829 ; MTBMA_c12410 .
    GeneIDi 9704949.
    KEGGi mmg:MTBMA_c12410.

    Phylogenomic databases

    HOGENOMi HOG000284153.
    KOi K14656.
    OMAi IVLGHDQ.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci MMAR79929:GH5J-1244-MONOMER.

    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

    1. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
      Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
      J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiRIBL_METTM
    AccessioniPrimary (citable) accession number: D9PX81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 27 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